Respiratory pigments

Keilin, D. (1925). On cytochrome, a respiratory pigment common to animals, yeasts and higher Plants. Proc. Roy. Soc. B 98, 312-329. 

High concentration of vanadium in the blood of some tunicates has been a long-standing problem of biochemistry. That vanadium(III) ions are part of the respiratory pigment has been ruled out recently. The efficient mechanism used to concentrate vanadium from sea water is now understood but the utility of vanadium for these living organisms is still an intriguing question. 

I must admit that this first visual perception of an intracellular respiratory process was one of the most impressive spectacles I have witnessed in the course of my work. Now I have no doubt that cytochrome is not only widely distributed in nature and completely independent of haemoglobin, but that it is an intracellular respiratory pigment which is much more important than haemoglobin. 

Biochemical evolution refers to changes over geologic time of the fundamental composition of organic components—e.g., the sequence of amino acids in protein molecules. The best documented example of biochemical evolution is that of the respiratory pigment haemoglobin, and the relation of its evolution to the fossil record has been summarized recently (58). Many of the monographs on comparative biochemistry have discussed biochemical evolution (59, 60, 61), and the reader is... 

Chlorins are the respiratory pigments in plants, and haemoglobin the respiratory pigment in the higher animals 62,64)-... 

Respiratory pigments similar to the vertebrate haemoglobins have also been identified in many invertebrates. These vary from small proteins with two Fe-porphyrin units to large molecules containing up to 190 Fe-porphyrin units. Myoglobin, the 02 storage protein in muscle tissue, is also a small iron-protoporphyrin protein. The crystal structures of this and a number of other porphyrin proteins are now known (Chapter 20.2, Table 11). 

Keilin D (1925) On cytochrome, a respiratory pigment, common to animals, yeast, and higher plants. Proc R Soc Lond B 98 312-339... 

In 1886, MacMunn 12) discovered the respiratory pigment, myohema-tin, which was widely distributed in plant and animal tissues. This important observation attracted little attention at the time of its publication and became effectively lost in the literature 13). In 1925, Keilin 14)... 

The first indication that copper is an essential body constituent, at least in some species, came with the recognition of the copper-containing respiratory pigment hemocyanin in cold-blooded animals (F8), and the discovery of turacin, a copper-containing pigment in the feathers of certain birds (CIO). 

Weber, R. E. (1978). Respiratory pigments. In Physiology of Annelids, ed. P. J. Mill. London Academic Press, pp. 393-446. 

Chance B (1952). Spectra and related kinetics of respiratory pigments of homogenized and intact cells. Nature, 16, 215-221. 

Dioxygen combines reversibly with Hb and Mb in the blood and tissues by virtue of a heme [iron(II) porphyrin] prosthetic group. The proteins bind one O2 for each Fe(Il). For this class of respiratory pigments, the Fe(II) is coordinated to the four core N atoms of the protoporphyrin (1). 

Hemerythrin is an oxygen carrier iron protein found in certain species of marine invertebrates within the Annelida, Brachiopoda, Priapulida and Sipunculoidea. This respiratory pigment can be considered a rather remote non-haem evolutionary relative of haemoglobin. It binds one... 

N4 mol wt 310.34. C 77.407 , H 4.55%, N 18.06%. Parent substance of the porphyrins, a group of compounds found in all living matter which are the basis of respiratory pigments in animals and plants. In porphyrins, side chains are substi -luted for the hydrogens in the porphine pyrrole rings. Chfo-rins are dihydroporphyrins. See also chlorophyll, hemoglobin, vitamin Bl . hematin. Prepn of porphine Fischer,... 

Tyrosinase is classified into the type-3 copper protein family, as are catechol oxidase and the respiratory pigment hemocyanin. During the catalytic reaction, the type-3 copper center of tyrosinase exists in three redox forms. The deoxy form (Cu(I)-Cu(I)) is a reduced species, which binds oxygen to give the oxy form (Cu(II)-02 -Cu(II)). In the oxy form, molecular oxygen is bound as peroxide in a side-on bridging mode, which destabilizes the... 

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