E. Newton Harvey

One of the most extraordinary things regarding luminescence in general is the small amount of material necessary to cause a visible emission of light. To take an extreme case, the flash of light resulting from the impact on ZnS of a single a particle, a helium atom, is visible to the naked eye. Addition of one part in a million of some heavy metal to pure CaS will confer phosphorescent properties on the latter. We are forced to believe that the heavy metal enters into some reaction during illumination which is reversed with light emission after illumination and a very small amount of heavy metal is necessary. Pyrogallol in water, 1:5,000,000 (m/512,000), can be oxidized with light production by K₄Fe(CN)₆ and H₂O₂ (Harvey, 1917) and m/100 pyrogallol + H₂O₂ will give a visible light with colloidal platinum in 1:250,000 concentration (Goss, 1917).

Luciferin and luciferase from Cypridina will also luminesce in exceedingly small concentration. If one grinds a single Cypridina in a mortar with water and dilutes the extract to 25,600 c.c., light can be observed if luciferin is added to this dilute luciferase solution. By determining the volume of the luminous gland of Cypridina and even assuming that this volume is all luciferase, one can calculate that one part of luciferase in 1,700,000,000 parts of water will give light when luciferin is added. Likewise, a similar dilution of luciferin will give visible light when luciferase is added.

The sensitivity of our eye is largely responsible for the detection of so small an energy change. As we have seen, recent determinations have proved that the dark adapted eye can detect 18 × 10^-10 ergs per second. From the heat of complete oxidation of pyrogallol it is possible to calculate the amount of pyrogallol necessary to give 18 × 10^-10 ergs if completely oxidized. This quantity is infinitesimally small. When pyrogallol is oxidized by K₄Fe(CN)₆ and H₂O₂, it is not completely oxidized and probably only a small amount of the energy is converted into light; otherwise we should be able to see the luminescence of a very much weaker concentration of pyrogallol. As the reaction luciferin ? oxyluciferin is so easily reversible, very little energy must be liberated, and, as experiments indicate, very little heat, if any, accompanies light production. Even though this be true, it is still possible for a very small amount of luciferin to produce a very large amount of light.

A very small amount of luciferase only is necessary because it behaves as an enzyme and follows the general rule that catalysts act in minute concentrations.

On the assumption that luciferase is an enzyme, an organic catalyst oxidizing luciferin with light production, we may appropriately inquire into the relation between the concentration of luciferin and luciferase and intensity and duration of luminescence. Oxygen tension, hydrogen ion concentration and temperature must be maintained constant as these all affect both intensity and duration of luminescence. Before considering luciferin and luciferase, however, let us study a few well-known chemiluminescent oxidations with special reference to concentration of reacting substances and temperature.

The effect of temperature on luminescence is of special interest because it gives us a means of analysis for determining if the luminescence depends on reaction velocity. We know that photochemical reactions are very little affected by temperature because the reaction is dependent on the absorption of light, a physical process, and this increases only a small per cent. for a rise of temperature of 10° C. To put it in the usual way, its temperature coefficient (Q₁₀) for a 10° interval is usually less than 1.1. On the other hand, we should expect photogenic reactions, in which some of the chemical energy is converted into radiant energy, to give off much more light the greater the reaction velocity. As reaction velocity increases so rapidly with temperature (Q₁₀ = 2 to 3), luminescence intensity should rapidly increase with increase in temperature.

Trautz (1905), from his extensive study of the chemiluminescence of phenol and aldehyde compounds came to the conclusion that luminescence intensity was proportional to reaction velocity. He based his conclusions largely on the effects of temperature and concentration of reacting substances and went so far as to declare that any reaction would produce luminescence if the reaction velocity were sufficiently increased. It is quite true that increasing the temperature does increase the intensity of chemiluminescence, but this is only within certain limits. As we raise the temperature, chemiluminescence becomes more intense but we soon reach a temperature for maximum luminescence and above this the intensity diminishes. This is especially well seen in the action of various oxidizers on pyrogallol and H₂O₂ recorded in Table 10. At 100° C. practically no light is produced by many oxidizers which are themselves unaffected at 100°. If we are to connect reaction velocity with intensity of luminescence we must conclude that the evolution of light is dependent rather on an optimum than a maximum reaction velocity.

TABLE 10
Temperature and Light Production. The Oxidizer is Mixed with an Equal Amount of M/100 Pyrogallol + 3 per cent. H₂O₂

Oxidizer	Temperatures
	0-2°	20°	50°	75°	98-100°
Turnip juice	Faint	Good	Good	Bright	Negative.
1 per cent. blood extract	Faint	Fair	Good		Fair.
m/20 K4Fe(CN)6	Negative	Good	Bright		Good.
m/100 KMnO4	Fair	Good	Bright	Bright	Faint flash.
m/50 K2Cr2O7	Negative	Fair	Faint	Fair	Negative.
m/100 CrO3	Negative	Good	Bright	Bright	Faint.
m/10 KCr alum	Negative	Faint	Faint	Faint	Negative.
m/10 NH4Fe alum	Negative	Faint	Faint	Faint	Very faint.
MnO2	Negative	Fair	Fair	Fair	Negative.
NaClO	Bright flash	Bright flash	Bright flash		Fair flash.

Quite a number of instances are known in which increasing the mass of reacting substances leads not to an increase but to an actual cessation of luminescence. This fact does not confirm the theory that reaction velocity is a determining factor in luminescence. The conditions for the luminescence of white phosphorus are most interesting and unusual. (See van't Hoff, 1895; Ewan, 1895; Centnerszwer, 1895; Russell,1903; Scharff, 1908.) Phosphorus will only begin to luminesce at a certain small pressure of oxygen. This "minimum luminescence pressure" of oxygen is very low, so low that earlier observers, failing to remove traces of oxygen, thought that luminescence might occur in absence of oxygen. Curiously enough there is also a "maximum luminescence pressure" of oxygen above which no luminescence occurs. Phosphorus will not luminesce in pure oxygen. Between the minimum and maximum is an "optimum luminescence pressure" where luminescence of the phosphorus is brightest. The exact values of these pressures vary with degree of water vapor present and with temperature. According to Abegg's Handbuch der anorganischen Chemie, the maximum luminescence pressure with water vapor present, is 320 mm. Hg at 0° and increases 13.19 mm. Hg for each degree rise in temperature. This means that for a definite temperature, say, 20°, phosphorus will not luminesce with an oxygen pressure of 583 mm. Hg, but will luminesce with pressures under this. If, however, we raise the temperature, luminescence will occur with an oxygen pressure of 583 mm. Hg.

A somewhat analogous case is presented by the oxidation of pyrogallol solution in contact with ozone, except that in this reaction too high a concentration of pyrogallol will hinder the oxidation. I have not studied the effect of varying concentrations of ozone. If oxygen, passed through an ozonizer (the silent electric discharge tube), is bubbled through m/100 pyrogallol, no luminescence occurs at 0°, a fair luminescence at 20°, a good luminescence at 50°, and a bright luminescence at the boiling point. If the pyrogallol is of m concentration, no luminescence occurs at 0° or 20°, a fair luminescence at 50°, and a bright luminescence at the boiling point. For a definite temperature, say 20°, no light appears if the pyrogallol is of m concentration, but if we raise the temperature, luminescence can occur. The similarity to phosphorus is obvious. Thus the "maximum luminescence pressure" of pyrogallol increases with increase of temperature.

We have already seen that pyrogallol can also be oxidized, if H₂O₂ is present, by a great variety of substances, such as peroxidases of potato or turnip juice, hÆmoglobin, KMnO₄, K₄Fe(CN)₆, CrO₃, MnO₂, hypochlorites and hypobromites, or colloidal Pt and Ag. For convenience we may collectively speak of these as oxidizers. They are recorded in Table 13. No light occurs if H₂O₂is absent. In the case of some of these oxidizers pyrogallol will luminesce in dilute concentrations but not in strong. Also, dilute pyrogallol will luminesce with a dilute solution of oxidizer but not with a concentrated solution of oxidizer. The effect of rise in temperature in these cases also is to increase the "maximum luminescence concentration" of pyrogallol and the "maximum luminescence concentration" of oxidizer. Table 11 shows this effect of temperature with K₄Fe(CN)₆ and varying concentrations of pyrogallol, and Table 12 shows the effect of temperature with pyrogallol and varying concentrations of K₄Fe(CN)₆. Table 10 shows the relation between temperature and intensity of luminescence with pyrogallol and various oxidizers. The terms faint, fair, good, and bright are purely relative designations of brightness as estimated by the eye, for accurate measurements of weak intensities are very difficult to make.

From Table 10 it should be noted that the intensity of luminescence of pyrogallol oxidized with most oxidizers is actually less at the boiling point, a fact which I have repeatedly verified. Let us now see how these facts are to be explained. If we assume that luminescence is dependent on reaction velocity, the intensity of luminescence should increase with increasing temperature. Up to a certain limit this is what we find, but at temperatures above this limit the intensity of luminescence actually decreases. The duration of luminescence also decreases. There is an optimum temperature for luminescence in many cases and we can only conclude that luminescence depends not on a very rapid reaction velocity but on a certain definite reaction velocity. Assuming that this is true, how can we account for the anomalous fact that in high concentrations of oxygen, phosphorus will not luminesce or that in high concentrations of pyrogallol, there is no luminescence in presence of ozone or of oxidizer and H₂O₂. Of course with high active mass of oxygen (in case of phosphorous luminescence) or of pyrogallol (in case of pyrogallol luminescence) the reaction velocity must be greater than the optimum. If that is the case, then lowering the temperature should reduce the reaction velocity to the optimum and light should appear. However, as we have seen, not lowering but raising the temperature causes luminescence with high oxygen concentration or high pyrogallol concentration.

TABLE 11
Temperature, Concentration of Pyrogallol, and Light Production. An Equal Amount of m/20 K₄Fe(CN)₆ is Mixed with Pyrogallol + 3 per Cent H₂O₂

Concentration of pyrogallol (after mixing)	Temperatures
	0-2°	10°	20°	30°	50°	75°	98-100°
m/4	Negative	Negative	Good	Very faint	Faint	Fair	Faint
m/40	Negative	Faint	Faint	Faint	Good	Bright	Good
m/400	Faint	Fair	Good	Good	Good	Bright	Bright flash
m/4,000	Bright	Bright	Bright	Bright	Bright flash	Fair flash	Negative

I believe the explanation of these phenomena lies rather in another direction and that the effect of the temperature and concentration of reacting substances affects not only the reaction velocity but also the reaction products. While intensity of luminescence undoubtedly increases with increasing reaction velocity, the luminescence itself probably accompanies only one stage in the formation of a series of oxidation products. This stage is favored at a definite temperature and mass of reacting substances. Thus, in the oxidation of phosphorus several intermediate oxides are said to be formed. The oxidation takes place in steps and probably the luminescence is connected with only one of the steps in a chain of reactions. It is probable that a certain oxygen pressure and temperature favors that particular step at the expense of the others and so this oxygen concentration and temperature correspond to the optimum for luminescence.

The supposition that certain definite oxidation products of pyrogallol must be formed in order to produce light is borne out by the fact that pyrogallol must be oxidized in a particular way to obtain luminescence. The blackening of pyrogallol with absorption of oxygen in presence of alkali is a very well-known reaction, but luminescence does not accompany this type of oxidation. I have tried mixing all concentrations of pyrogallol and all concentrations of alkali in an endeavor to obtain some light, but always with negative results. Likewise my attempts to obtain light during the electrolysis of salt solutions containing pyrogallol by means of the nascent oxygen at various kinds of anodes have met with negative results. A similar case is presented by luciferin which oxidizes spontaneously (most rapidly in presence of alkali) without light production and only produces light when oxidized in presence of luciferase.

To sum up the results of the dynamics of chemiluminescence we may say that certain oxyluminescences occur only if the substance is oxidized in a particular way under definite conditions of temperature and concentration and that this is probably due to a favoring of one step (with which the luminescence is associated) in a chain of oxidations. Providing temperature and concentration are such as to favor the step responsible for luminescence, then higher temperature and greater concentration result in increased intensity of luminescence.

Let us now turn to luminous organisms and consider the effect of temperature and of concentration of reacting substances (oxygen, luciferin and luciferase) on the luminescence. We have already seen that luminescence of a luciferin-luciferase mixture begins with an extraordinarily low oxygen tension and increases in intensity with increasing tension of oxygen, but that very soon an oxygen tension is reached where a maximum luminescence is obtained and further increase of oxygen tension gives no brighter light. In this respect the luminescence intensity—oxygen tension curve is no doubt very similar to the hÆmoglobin saturation—oxygen tension curve. HÆmoglobin is about 50 per cent. saturated at 10 mm. oxygen pressure, 80 per cent. saturated at 20 mm. oxygen pressure and completely saturated at pressures of oxygen well below the pressure of oxygen in air (152 mm. Hg). As the optimum oxygen tension for luminescence of luciferin is also well below that of air, mixtures of luciferin and luciferase luminesce with equal brilliancy whether air or pure oxygen is bubbled through them. To obtain an excess of oxygen it is only necessary to keep the solution saturated with air and statements regarding concentration of luciferin and luciferase and intensity or duration refer to excess of oxygen. Investigators who have studied the effect of increase in oxygen pressure on luminous animals have come to the same conclusions. High pressures of air or oxygen do not increase the intensity of luminescence (Dubois and Regnard, 1884).

The hydrogen ion concentration of crude solutions of luciferin and luciferase, made by extracting whole Cypridinas with hot or cold water is fairly constant, about Ph = 9, determined electrometrically. Such solutions have a high buffer value and the Ph does not change during oxidation of luciferin so that this variable is automatically controlled.

Because of difficulties in measuring low intensities of light which are constantly changing, no figures on light intensities can be given, but it is easy to establish the following facts: The greater the concentration of luciferin or luciferase the more intense the luminescence. The greater the concentration of luciferin the longer the duration of luminescence and the greater the concentration of luciferase, the shorter the luminescence lasts. Thus, if we mix concentrated luciferin and weak luciferase we get a bright light which lasts for a half hour or more, gradually growing more dim. Concentrated luciferase and weak luciferin give a bright flash of light which disappears almost instantly. Concentrated luciferase and concentrated luciferin give a brilliant light which lasts for an intermediate length of time and weak luciferin and weak luciferase give a faint luminescence which lasts for an intermediate length of time.

These facts can all be explained by regarding luciferase as a catalyzer which accelerates the oxidation of luciferin and by assuming that intensity of luminescence is dependent on reaction velocity, i.e., on rate of oxidation. Contrary to the condition for phosphorus and for pyrogallol there appears to be no optimum concentration of luciferase or luciferin, but the luminescence intensity increases gradually with increasing concentration of luminous substances up to the point where pure (?) luciferin and pure (?) luciferase, as secreted from the gland cells of the animal, come in contact with each other. This, the maximum brightness, is not to be compared with the light of an incandescent solid, but is nevertheless visible in a well-lighted room, out of direct sunlight.

The effect of temperature on Cypridina luminescence also bears out the preceding conclusions. For a given mixture of luciferin and luciferase the light becomes more intense with increasing temperature up to a definite optimum and then diminishes in intensity. The diminution in intensity above the optimum is due to a reversible change in the luciferase so that its active mass diminishes. This change becomes irreversible in the neighborhood of 70° (depending on various conditions), where coagulation of luciferase occurs. Light will appear at 0° but it is far less intense than light at higher temperatures and it is more yellow in color. The light of optimum temperatures is quite blue. The weaker light at temperatures above the optimum is also more yellow in color. I believe this difference in color is a function of the slowed reaction velocity, for a mixture of luciferin and luciferase which gives a bluish luminescence at room temperature, will give a weaker and yellowish luminescence if diluted with water. Dilution with water will slow the reaction velocity. If the difference in color were not real but due to change in color sensitivity of the eye with different intensities of such relatively weak light (Purkinje phenomenon), the weaker light should appear more blue. As the weaker light appears more yellow, I therefore believe the color difference is actual and not subjective.

A minimum, optimum, and maximum temperature for luminescence is observed in all luminous organisms. The minimum is usually very low. Luminous bacteria will still light at -11.5° C. The power to luminesce under ordinary conditions is not destroyed by exposure to liquid air, for, on raising the temperature, light again appears (Macfayden, 1900, 1902). Almost all organisms will luminesce at 0° C., and the luminescence minimum probably represents the point at which complete freezing of the luminous solution occurs. It is very low with bacteria because they are solutions in capillary spaces of very small size, a condition tending to lower the freezing point.

The luminescence maximum represents the point at which luciferase is reversibly changed so as to be no longer active. If the temperature is again lowered the luciferase again becomes active and light reappears. Some degrees above this, and in all forms well below the boiling point, luciferase is coagulated and destroyed. As the coagulation point of proteins depends on many factors, such as time of heating, salt content, acidity, etc., so the luciferases of different animals coagulate at different temperatures depending on these conditions. Some of the more reliable observations on these critical temperatures are collected in Table 14.

We are thus led to the conclusion that intensity of luminescence is dependent on the velocity of oxidation of luciferin and that with lowered reaction velocity the spectral composition of the light changes. The maximum emission shifts toward the yellow. I believe, however, that in Cypridina also, the luminescence intensity depends not only on reaction velocity but on the particular manner in which luciferin is oxidized. Cypridina luciferin will luminesce only in presence of Cypridina luciferase and no light can be obtained from Cypridina luciferin and a host of different oxidizers (with or without H₂O₂) such as are able to oxidize pyrogallol. Luciferin will also oxidize in the air spontaneously but no light is produced. It is easy to show that this spontaneous oxidation may be much more rapid than an oxidation with luciferase and yet light appears only in presence of the latter. If a concentrated solution of luciferin is kept near the boiling point it will be completely oxidized to oxyluciferin in four or five minutes. No light appears if air or even if pure oxygen is bubbled through it. The same solution kept at 20° with a small amount of luciferase will luminesce continuously and not be completely oxidized to oxyluciferin in a half hour. We can, however, cause the luciferin to oxidize as rapidly at 20° by adding concentrated luciferase as does the luciferin near the boiling point without luciferase. A bright light is produced in the former case, none in the latter case. The oxyluciferin formed from spontaneous oxidation of luciferin appears to be the same as that formed with luciferase present. Both give luciferin again on reduction. Perhaps the reaction takes place in two stages, similar to those supposed to occur in other enzyme actions:

luciferin + luciferase = luciferinluciferase

luciferinluciferase + O (or minus H₂) = oxyluciferin + luciferase.

We may then assume as a tentative hypothesis that luminescence only occurs during oxidation (addition of O or removal of H) of the luciferinluciferase compound.

We have just seen that the effect of cooling a Cypridina extract containing luciferin and luciferase and luminescing with a bluish light, is to reduce the intensity and change the shade toward the yellow. Velocity of oxidation must be lowered and with the same concentration of luciferase lowered velocity means more light of the longer wave-lengths. A very instructive experiment on color of the light can be carried out with animals having different colored lights and so closely related that their luciferins and luciferases will interact with each other. Such a case is presented by the American fireflies, Photinus and Photuris. Photinus emits an orange light, while Photuris emits a greenish yellow light. The difference in color is especially noticeable when the luminous organs of the two forms are ground up in separate mortars. As shown by Coblentz, the difference in color is real, the spectrum of Photinus extending farther into the red than that of Photuris (see Fig. 8). We can easily prepare luciferin and luciferase from the two fireflies and make the following mixtures:

Photinus luciferin × Photinus luciferase = reddish light.

Photinus luciferin × Photuris luciferase = yellowish light.

Photuris luciferin × Photuris luciferase = yellowish light.

Photuris luciferin × Photinus luciferase = reddish light.

Thus the color of the light in these "crosses" is that characteristic of the animal supplying the luciferase. To bring this fact in line with what we have already said regarding reaction velocity and luminescence, we must believe that the Photinus luciferase oxidizes at a slower rate than the Photuris luciferase. In this connection it is of interest to recall that the Photuris light as emitted by the insect becomes reddish at high temperatures, or if the insect is plunged into alcohol, both conditions which bring about partial coagulation of the luciferase and reduce its active mass.

BIBLIOGRAPHY

A few of the enormous number of papers on luminescence are included in the list below. The attempt is made to list only those dealing with the structure, chemistry or physiology of luminous animals and the physical nature of their light, together with a small number of general interest. More complete works on light and luminescence come first and original articles follow. Authors' names are arranged alphabetically, their papers chronologically. A fairly complete list of literature covering the whole field of Bioluminescence is given by Mangold, 1910. The 1913 paper of Dubois gives a bibliography of his own contributions up to this date so that only those papers to which special reference is made are included below.

BOOKS AND GENERAL WORKS

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Dahlgren, U.: 1915, The Production of Light by Animals. Jour. Franklin Inst., vols. 180 to date.

Dubois, R.: 1914, La Vie et La LumiÈre. Alcan, Paris.

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Harvey, E. N.: 1917, The Chemistry of Light Production in Luminous Organisms. Carnegie Inst., Wash., Pub. No. 251, pages 171-234.

Heinrich, Pl.: 1811-1820, Die Phosphorescenz der KÖrper, etc. NÜrnburg.

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Original Papers

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INDEX

• Abegg, R., 147
• Acanthephyra, 78
• Agaricus, 99
• Agassiz, A., 11
• Alkaptonuria, 17
• Allman, G. I., 11, 71
• Ammonia, 12
• Anodoluminescence, 26, 29
• Anornalops, 69
• Aristeus, 72
• Aristotle, 1

• Bach, A., 137
• Bacteria, luminous, 2, 10, 13, 14, 16, 18, 28, 45, 53, 61, 65, 69, 72, 74, 81, 82, 89, 99, 101, 103
• Bacterial lamps, 18
• Baker, J., 2
• Bancroft, W. D., 36
• Bancroft and Weiser, 24
• Bandrowski, E., 33
• Barcroft and Hill, 98
• Barnea, 116
• Batelli and Stern, 115
• Becquerel, E., 26
• Beijerinck, M. W., 18, 89, 99, 100, 102
• Bigelow, S. L., 34
• Black, 91
• Bolitophila, 77
• Boyle, R., 1, 16, 85 ff
• Brandt, 36
• Brittle stars or ophiuroids, 10, 11, 72

• Canton's phosphorus, 27
• Carbon dioxide and luminescence, 91 ff
• Cardium, 116
• Cascariolo, V., 27
• Cathodoluminescence, 26, 29
• Cavernularia, 74, 103
• Centnerzwer, M., 147
• Cephalopods or Squid, 10, 11, 13, 68, 72, 84, 104
• Ceratium, 71
• ChÆtopterus, 10, 17, 42, 71, 73, 74, 83, 103
• Chemiluminescence, 36 ff, 45 ff
• Chlorophyll formation by animal light, 66
• Chromophyton, 15
• Chun, C., 79
• Coblentz, W. W., 30, 31, 44, 51, 52, 59, 60, 62, 64, 93, 160.
• Co-enzyme, 104, 130
• Co-luciferase, 107 ff
• Color of animal light, 41 ff, 157 ff
• Concentration and luminiscence, 145 ff
• Conroy, J., 43
• Crozier, W. J., 71, 103
• Crustacea, 10, 14, 68, 70, 72, 89, 101 ff
• Crysalloluminescence, 33 ff, 74
• Ctenophores, 2, 10, 11, 71, 72, 82
• Cyanides and luminescence, 126
• Cypridina, 14, 30, 45, 48, 63, 71, 73, 75 ff, 90, 92, 98, 103, 105 ff, 155 ff

• Dahlgren, U., 72, 73, 75
• "Death Glow," 69
• Dinoflagellates, 2, 10, 32, 82
• Dubois, R., 31, 35, 37, 43, 45, 49, 61, 64, 73, 103 ff, 111, 114 ff, 131, 155

• Earthworms, 10
• Efficiency of animal light, 48 ff
• Eggs, luminous, 11
• Electroluminescence, 24, 29
• Embryos, luminous, 11
• Euphasia, 72
• Ewan, T., 147
• Exner, S., 30
• Extracellular luminescence, 68, 71
• Eyes, luminous, 15 ff

• Fabre J. H., 99
• Fahrig, E., 37
• Fireflies, 10, 31, 34, 43, 69, 71, 77 ff, 89, 93, 101, 103, 135, 160
• Fishes, 1, 3, 10, 18, 64, 69, 72, 84, 85
• Flowers, flashing of, 16
• Fluorescence, 25 ff, 62
• Fluorescent screens, 29
• Forsyth, R. W., 53
• Frankland, P., 62
• Friedberger & Doepner, 65
• Frogs, luminous, 13
• Fungi or Basidiomycetes, 10, 69, 72, 81, 89, 99, 101

• Galloway and Welch, 84
• Gernez, D., 32
• Giard and Billet, 13
• Giesbrecht, W., 11, 70
• Glowworms, 1, 10, 43, 77
• Gnathophausia, 72
• Goss, B. C., 143
• Greene, C. W., 70
• Guinchant, 37

• H-ion concentration and luminescence, 92, 138, 155
• Heat production and luminescence, 93 ff
• Heliotropism by animal light, 66.
• Heller, J. F., 1, 2, 16
• Heterocarpus, 72
• Heteroteuthis, 72
• Hooke, R., 91
• Hulme, N., 1
• Hyde, Forsyth and Cady, 57, 63
• Hydrogenase, 131
• Hydroils, 10, 72

• "Ignis fatuus," 15
• Immune bodies, 104
• Infection, with luminous bacteria, 13
• Infra red rays in animal light, 48 ff
• Intensity of animal light, 63
• Intracellular Luminescence, 68, 71
• Interference colors, 14
• Issatschenko, B., 66
• Ives, H. E., 28, 44, 51 ff, 59, 61

• Kemp, C., 78

• Langley and Very, 43, 50 ff, 64
• Lankester, E. R., 42
• Lavoisier, 91
• Lenard and Wolf, 37
• Ligia, 13
• Limulus, 129
• Linnemann, E., 36
• Lode, A., 65
• Luciferase, 103 ff. Chap VI (properties);
• of Pholas, 114;
• of Cypridina, 123 ff
• Luciferesceine, 31, 110
• Luciferin, 103 ff. Chap. VI (properties);
• of Pholas, 114;
• of Cypridina, 116 ff
• Luciola, 103, 125.
• Luminescence, 23 ff
• Luminosity, distribution in plant and animal kingdom, 3 to 12
• Luminosity, false, 12 ff
• Luminous animals, habitat, 10
• Luminous animals, uses of to man, 17 ff
• Luminous granules, 73, 75
• Lyman rays, 21
• Lyoluminescence, 35

• MacCartney, J., 2, 3
• Macfayden, A., 157
• Macrozymases, 73
• Man, luminosity of, 16
• Mangold, E., 11, 72
• Massart, J., 71
• Mast, S. O., 69
• Mayow, 91
• McDermott, F. A., 31, 37, 45, 53
• McKenney, R. B., 100
• MedusÆ or jelly fish, 2, 10, 72, 82
• Methane, 15.
• Michaelis, G. A., 1
• "Minimum radiation visually perceptible," 65, 144
• Molisch, H., 45, 53, 61, 66, 102
• Molluscs, 10, 72
• Monocentris, 69, 104
• Moore, B., 71
• Muraoka, H., 61
• Myriapods, 10, 2
• Sepietta, 72
• Sergestes, 72, 78
• Singh and Maulik, 61
• Solen, 116
• Spallanzani, L., 85, 101
• Spectrum of chemiluminescence, 39
• Spectrum of luminous organisms, 42 ff
• Spectrum of phosphorescence, 28
• Spectrum, range of, 21 ff
• Spinthariscope, 30
• Steche, O., 65, 69
• Stefan-Boltzmann Law, 22, 23
• Stimulation and luminescence, 68 ff, 135
• Stoke's Law, 28, 31
• Stylochiron, 72
• Suchsland, E., 61
• Sulphides, phosphorescence of, 27
• Sweat, luminous, 17

• Talitrus, 13
• Tarchanoff, J., 13
• Temperature and luminescence, 145 ff, 156 ff
• Temperature radiation, 23
• Thaumatolampas, 42
• Thermoluminescence, 24 ff
• Tomopterus, 72
• Transparency of chitin to infra-red, 52
• Trautz, M., 32, 33, 37, 39, 145
• Triboluminescence, 32 ff
• Trojan, E., 11, 78
• Tschugaeff, L., 32

• Ultra violet rays in animal light, 53 ff
• Urine, luminous, 18
• Uses of luminous organs, 81 ff

• Vacuolides, 73
• van Helmont, 91
• van't Hoff, J. H., 147
• Vibrio, 65
• Ville and Derrien, 111
• Visual sensibility, 54 ff

• Watanabe, H., 75
• Watasenia, 104
• Water and luminescence, 85, 101
• Weiser, H. B., 33, 34, 39
• Welker, W. H., 121
• Wheeler and Williams, 77
• Wiedemann, E., 23
• Wiedemann and Schmidt, 25, 36
• "Will-o'-the-wisp," 15
• Wood, phosphorescent or shining, 1,

  The spellings of "Sidot blend" and "Sidot blende" are used interchangeably.

  "PH" or P_H (subscript H) is used throughout for the scale of alkali-acidity where the modern usage is "pH".

  On page 173, the citation for Nutting, P. G.: 1908 has page range pp. 261-039. This is as it appears in the original, but is probably in error.

  Minor corrections to formatting and missing punctuation (mostly in the bibliography) have been changed without an explicit note.

  ---

  Changes to the text have been made only in the case of obvious spelling or type-setting errors. These are listed as follows:

  Page ix: changed "Phoshorescence" to "Phosphorescence" (II. Luminescence and Incandescence ... Phosphorescence and fluorescence.)

  Page ix: changed "Biozymoxyluminescence" to "BiozymoÖxyluminescence" (V. The Chemistry of Light Production, Part I ... "BiozymoÖxyluminescence.")

  Page x: changed "chemi-luminescence" to "chemiluminescence" in two instances (Reaction velocity and chemiluminescence. Temperature and chemiluminescence.)

  Page 15: changed "th" to "the" (Less well known is the Ignis fatuus)

  Page 26: re-positioned period outside of parentheses "after being illuminated (photoluminescence)."

  Page 29: changed "platino-cyanide" to "platinocyanide" (Fluorescent screens of barium platinocyanide)

  Page 29: added missing comma (willemite (Zn₂SiO₄), Sidot blend)

  Page 34: added missing closing quotation mark ("It is altogether probable that the cause of this" ...)

  Page 39: superscript "2" changed to subscript "2" in Na₂CO₃ (the pyrogallol-formaldehyde-Na₂CO₃-H₂O₂ reaction).

  Page 41: "50-metre candles" changed to "50 metre-candles" (Below 0.5 and above 50 metre-candles visibility varies ...)

  Page 42, Table 4: changed "FraÜnhofer" to "Fraunhofer" in the caption and table heading (Fraunhofer Lines)

  Page 47, Table 5: changed "Forster" to "FÖrster" (Bacteria ... FÖrster, 1887)

  Page 56, Fig 12 caption: "Forsythe" changed to "Forsyth" (after Hyde, Forsyth and Cady).

  Page 72: added missing closing parenthesis "the molluscs (Pholas and PhyllirhoË)".

  Page 74: "secretion" changed to "section" (A section of the epithelium shows large mucous-producing cells ...)

  Page 75: added missing closing punctuation (At least one, probably two, are concerned in light production.)

  Page 75: changed "intra-cellular" to "intracellular" (animals possessing light cells with intracellular luminescence)

  Page 81; Fig. 29 caption: added missing comma (chr.¹, chromatophore; ...)

  Page 87: added missing closing parenthesis "(and that too of such a Density to make them continue shining)."

  Page 90: "necesary" changed to "necessary" (Boyle also made many experiments to show that air was necessary for the life of animals ...)

  Page 93: changed "thermo-couple" to "thermocouple" (using a thermocouple as the measuring instrument)

  Page 94: "D" changed to "B" (placed in a large Dewar flask (B) filled with water)

  Page 94: "Thermo-couples" changed to "Thermocouples" (Thermocouples (L and M) of advance...)

  Page 97: "thermo-couple" changed to "thermocouple" (Readings of each thermocouple on the galvanometer scale ...)

  Page 100: changed "McKenny" to "McKenney" (McKenney (1902) found also ...)

  Page 102: changed "misceable" to "miscible" (insoluble in water but miscible with it)

  Page 103: "demontrate" changed to "demonstrate" (I have been unable to demonstrate their existence in luminous bacteria;)

  Page 104: "thermolable" changed to "thermolabile" ( ...and a thermolabile complement (alexin) are necessary.)

  Page 104: "thermolable" changed to "thermolabile" (Because of the necessity of thermostable and thermolabile substances for light production ...)

  Page 105: "thermolable" changed to "thermolabile" (luciferase (=photogenin) for the thermolabile material ...)

  Page 111: "preslence and H₂O₃" changed to "presence of H₂O₂" (lophin could be oxidized by vertebrate blood in the presence of H₂O₂.)

  Page 116: "or" changed to "of" ( ... and would disappear from solution in the course of a day or so.)

  Page 116: changed "oxidizible" to "oxidizable" (The luciferins, as the oxidizable substances, must claim first attention.)

  Page 123: "contrated" changed to "concentrated" (1 c.c. portions of concentrated luciferin)

  Page 132: "coluciferase" changed to "co-luciferase" (He now regards it as identical with his co-luciferase)

  Page 151, Table 13: corrected duplicate numbering "10" to "11" (11 Ferric chloride)

  Page 151, Table 13: corrected duplicate numbering "14" to "15" (15 Chromic sulfate)

  Page 151, Table 13: abbreviated "minute" to "min." in two entries (boiled 1 min. and filtered)

  Page 158: changed "appear" to "appears" (... and yet light appears only in presence of the latter.)

  Page 162: added missing closing punctuation (More complete works on light and luminescence come first and original articles follow.)

  Page 165: added missing comma (Dubois, R.: 1918a, Sur la SynthÈse de la Luciferine.)

  Page 165: changed "BiophotogÉnesis" to "BiophotogÉnÈse" (Recherches Recentes de M. Newton Harvey sur la BiophotogÉnÈse)

  Page 165: changed "BiophotogÉnÈsis" to "BiophotogÉnÈse" (Nouvelles Recherches sur la BiophotogÉnÈse)

  Page 166: changed "Oxydations geschwindigkeit" to "Oxydationsgeschwindigkeit" (Ueber die Oxydationsgeschwindigkeit von Phosphor ...)

  Page 166: changed "Radiumstrahlem" to "Radiumstrahlen" (Einige Beobachtungen ueber die durch Radiumstrahlen in den tierischen Geweben erzeugte Phosphoreszenz.)

  Page 166: changed "neiderer" to "niederer" (Ueber die Entwicklung von Bakterien bei niederer Temperatur.)

  Page 167: changed "nueue" to "neue" (Ueber die rosettenfÖrmigen Leuchtorgane der Tomopteriden und zwei neue Arten von Tomopteris.)

  Page 169: added missing hyphen to "Pflanzen-" (Ueber das Leuchten im Pflanzen-und Tierreiche.)

  Page 169: changed "Rucksicht" to "RÜcksicht" (mit bes. RÜcksicht auf. med. Diagnost. u. Therapie Wien.)

  Page 170: changed "jord." to "jard." (Bull. d. jard. imp. botan. St. Petersburg)

  Page 171: changed "LichtfaÜle" to "LichtfÄule" (Phosphorezierende TausendfÜssler und die LichtfÄule des Holzes)

  Page 172: changed "Pfluger's Arch" to "PflÜger's Arch." (PflÜger's Arch., Bd. cxix, pp. 583-601.)

  Page 174: changed "Bedentung" to "Bedeutung" ( ... ihre Bedeutung fÜr die Principien der Respiration)

  Page 175: changed "Lazaro" to "Lazzaro" (Spallanzani, Lazzaro: 1794, ...)

  Page 176: changed "Leuchtvermogen" to "LeuchtvermÖgen" (Ueber das LeuchtvermÖgen von Amphiura squamata, Sars.)

  Page 177: changed "Triboluminescenz" to "Tribolumineszenz" (Tschugaeff, L.: 1901, Ueber Tribolumineszenz.)

  Page 179: changed "Bandromski" to "Bandrowski" (Bandrowski, E., 33)

  Page 179: changed "Baelli" to "Batelli" (Batelli and Stern, 115)

  Page 179: changed "Centnerswer" to "Centnerzwer" (Centnerzwer, M., 147)

  Page 179: changed "Fire-flies" to "Fireflies" (Fireflies, 10, 31, 34,...)

  Page 180: changed "Forsythe" to "Forsyth" (Hyde, Forsyth and Cady, 57, 63).

  Page 180: changed "Flankland" to "Frankland" (Frankland, P., 62)

  Page 180: changed "Glow-worms" to "Glowworms" (Glowworms, 1, 10, 43, 77)

  Page 181: changed "Piezolumisescence" to "Piezoluminescence" (Piezoluminescence, 32 ff).

  Page 182: changed "Stefan-Boltzman" to "Stefan-Boltzmann" (Stefan-Boltzmann Law, 22, 23)

  Page 182: changed "infrared" to "infra-red" (Transparency of chitin to infra-red, 52)

  Page 182: added missing page references (Weiser, H. B., 33, 34, 39).

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