Hemoglobin: Its Occurrence, Structure, and Adaptation N. M. Senozan and R. L. Hunt California State University, Long Beach, CA 90840 In the animal kingdom, oxygen is transported by three metal-containine known as hemervthrin, hemocy-nroteins . anin, and hemoglobin. Although the heme prefix appears in all three names, only hemoglobin actually has a heme group (Figure 1j. Hemerythrin and hemocyanin are nonheme comoounds in which the metal is bound directly to the protein (1-5). Hemerythrin contains iron and occurs in four phyla of rather obscure marine animals. Hemocyanin, a copper protein, has, in a sense, an even more limited distribution. I t is found only in certain mollusks and arthropods. Included in these two phyla, however, are some of the most awesome and fascinating creatures of the oceans. The large and terrifying squids of the Humboldt Current, the octopus, as well as lobsters, crabs, shrimp, and many spiders and scorpions, depend on hemocyanin for their respiration ( 6 4 ) . Hemoglobin, the most widely distrihuted of the three carriers, comes in a variety of forms (Figure 2). In its simplest version, it consists of a heme and a single polypeptide chain, about 150 amino acids long, wrapped around the heme. Such monomeric hemoelobins. when found in muscle cells, are called myoglohin."They store oxygen and help promote its transfer from blood to mitochondria (9.10). Aquatic mammals - -
in color" (I fi. Monomeric hernoelohins also occur in the blood of invertebrates and in the roots of legumes such as soybean. The latter is known as leghemoglobin and provides an important ~ alhurlmlg ,l*\.Avn :111dc rt ,111111 311.In.vr\.~t.tr z r Ill( I ) ~ , # I Iny , x d ~ i cm t ~ d i u ~e.3~ n l i t i , J ts~rr l l v w,rkin< ~ i i r r , w ~ ~:I: ~ key ~v. enzyme in nitrogen fixation (12,131. In vertebrate blood, with few exceptions, hemoglobin is present as a tetrameric molecule made of four myoglohin-like subunits. In invertebrates the situation is quite complex (14). Some animals such as the larval form of midre - Chironomus have simple hemoglobins, either monomeric or made of a few suhunits. In others. ex.. in the earthworm Lumbricus, extensive aggregation takes place and molecular weights exceeding 3 X 1 0 b r e encountered. These high molecular weight hemoglobins, which may contain up to 200 hemes per molecule. are also called ervthrocruorins. One form of erythrocruoiin that will be discussed later is known as chlorocruorin, nresumablv because of its unusual green color. Unlike simple hemoglobihs, where each 16,000 g contains one mole of iron, for erythrocruorins and chlorocruorins the weight of pigment per mole of iron ranges from 20,000 to 30,000 g and in one case, the intestinal parasite Ascaris, reaches 40,000 g (15,161. With curious excention of the ice fish, a laree and almost - ~ -the ~transparent animal that dwells in the cold waters of Antarctica, and the larval form of a certain eel, all vertebrates have hemoglobin (14,17,18). Among invertebrates, however, the distribution is erratic and does not seem to follow anv evolutionary or environmental scheme. The sea cucumber, Mulpadia arenicola, for instance, bleeds profusely, hut its close relative the starfish does not contain hemoglobin or any other oxygen carrier (19). I t might he mentioned in passing that respiratory function has been attributed to a vanadium compound that occurs abundantly in sea squirts, a group of marine animals related to ~rimitivevertebrates (20). Recent evidence, however,
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Bonaventura, J. and Bonaventurs, C., Amei Zooi, 20,7 (1980). Magnum, C. P.,Amer. Zmi.,20, 19 (1980). Senosan, N. M., J. CHEMEDUC., 53,684 (1976). Antonini, E., and Brunori, M., "Hemaglobin and Myoglobin in their Reactions with Ligands," North~HoUandPublishing Company, Amsterdam, 1971. (10) Perutz,M. F., Sci. Amer ,239-246,92 (1978). (11) Kendrew, J. C., Parrish, R. G., Marrack, J. R., and Oriani. E. S.. Nature.. 174,. 946 (1954). (12) Wittenberg, J. B.,AppIeby, C. A . , B q e r m ~ , F J.,andTw~er, . G. L., Ann. N.Y. Acad. Sci.. 244,28 (1974). (13) Brill, W.J.,Sci. Amri.236-243.66 (19771. (141 Manwell, C.. Annu RODPhysi01, 22.191 (1960). (151 Terdliger, R. C., Amen Zooi., 20.53 (1980). (161 Chung, M. C. M., and Ellerton, H. D.. Prog Biophys. Mol. Biol., 35, 63 (1979). (17) Pr-r, C. L., "Compsrstiue AnlmdPhysiology," W. B. Saunderr Company, vhils~ ddphia, 1973. (18) Ruud. J . T.,Sci. Amor. 213-215.108 (19651. (191 Bonaventurx, C.. Bonaventura,J.. Kiito,B.,Brunori,M.,andAntonini,E..Riorhim Biophys. Acto.428.779 (19761. (20) Senozan, N. M.. J. CHEMEDUC., 51,503 (1974). (211 Crulson, R. M. K., Proc. Nat. Acod Sci. U.S.A., 72,2217 (1975). (221 Macara, I. G., McLed, G. C., and Kustin, K.. Comp. Biochrm. Physioi., 62A. 821 ilP"Gi ~.".",.
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