Summary
Hagfish hemoglobin has three main components, one of which is Hb III. It is monomeric and consists of 148 amino acid residues (M = 17 350). Its complete primary structure, previously published, is discussed here. The proximal amino acid (F8) of the heme linkage is histidine as always in the hemoglobins, but the regularly expected distal histidine E7 is substituted by glutamine. This substitution, leading to a new kind of heme linkage, has hitherto only been demonstrated in opossum hemoglobin. It is suggested that E7, Gln, is directed out of the heme pocket, and that the adjacent Ell, Ile, is directed toward the inside of the pocket, giving the distal heme contact instead of histidine.Myxine Hb III has an additional tail of 9 amino acid residues at its N-terminal end, as has the hemoglobin ofLampetra fluviatilis. The genetic codes ofMyxine andLampetra hemoglobins show 117 differences, in spite of many morphological resemblances between hagfish and lamprey. Their primary hemoglobin structures show differences substantial enough to bo compatible with the divergence of the two families some 400–500 million years ago.
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References
Bauer C, Engels U, Paléus S (1975) Nature 256:66–68
Braunitzer G, Fujiki H (1969) Naturwissenschaften 56:322–323
Braunitzer G, Schrank B, Stangl A, Bauer C (1978a) Hoppe-Seyler's Z Physiol Chem 359:547–558
Braunitzer G, Schrank B, Stangl A, Scheithauer U (1978b) Hoppe-Seyler's Z Physiol Chem 359:137–146
Braunitzer G, Gehring-Müller R, Hilschmann N, Hilse K, Hobom G, Rudloff V, Wittmann-Liebold B (1961) Hoppe-Seyler's Z Physiol Chem 325:283–286
Briehl R (1963) J Biol Chem 238:2361–2366
Buse G, Braig S, Braunitzer G (1969) Hoppe-Seyler's Z Physiol Chem 350:1686–1690
Chauvet JP, Acher R (1970a) FEBS Lett 8:263–264
Chauvet JP, Acher R (1970b) FEBS Lett 9:202–204
Edmundson AB (1965) Nature 205:883–887
Fermi G (1975) J Mol Biol 97:237–256
Gerald PS, Efron ML (1961) Proc Natl Acad Sci USA 47:1758–1767
Hendrickson WA, Love WE, Karle J (1973) J Mol Biol 74:331–361
Hilse K, Braunitzer G (1968) Hoppe-Seyler's Z Physiol Chem 349:433–450
Huber R, Epp O, Steigemann W, Formanek H (1971) Eur J Biochem 19:42:50
Hunt LT, Dayhoff MO (1976) In: Dayhoff MO (ed) Atlas of Protein Sequence and Structure. National Biomedical Research Foundation, Georgetown University Medical Center, Washington, D.C. 20007, pp 191–233
Hörlein H, Weber G (1948) Dtsch Med Wochenschr 39:476–478
Imamura T, Baldwin TO, Riggs A (1972) J Biol Chem 247:2785–2797
Isaacks RE, Kim HD, Harkness DR (1978) Can J Zool 56:887–890
Jarvik E (1964) Ann Soc Roy Zool Belgique 94:11–95
Kleinschmidt T, Braunitzer G (1976) Hoppe-Seyler's Z Physiol Chem 357:1805–1808
Li SL, Riggs A (1970) J Biol Chem 245:6149–6169
Li SL, Riggs A (1972) J Mol Evol 1:208–210
Liljeqvist G, Braunitzer G, Paléus S (1979) Hoppe-Seyler's Z Physiol Chem 360:125–135
Manwell C (1963) In: Brodal A and Fänge R (eds) The Biology ofMyxine. Universitetsforlaget, Oslo, Norway, pp 372–455
Muirhead H, Perutz MF (1963) Nature 199:633–638
Muller CJ, Kingma S (1961) Biochim Biophys Acta 50:595
Nash AR, Fisher WK, Thompson EOP (1976) Aust J Biol Sci 29:73–97
Padlan EA, Love WE (1974) J Biol Chem 249:4067–4078
Paléus S, Vesterberg O (1966) Intern SympComparative Hemoglobin Structure, Thessaloniki, 11–13 April 1966, M. Triantafylou, Thessaloniki, pp 149–150
Paléus S, Liljeqvist G (1972) Comp Biochem Physiol 42B:611–617
Paléus S, Vesterberg O, Liljeqvist G (1971) Comp Biochem Physiol 39B:551–557
Perutz MF (1976) Br Med Bull 32:195–208
Perutz MF, Lehmann H (1968) Nature 219:902–909
Perutz MF, Muirhead H, Cox JM, Goaman LCG (1968) Naure 219:131–139
Quast R, Paléus S, Bloom G, Östlund E (1969) Acta Chem Scand 23:3595–3596
Romero Herrera AE, Lehmann H (1974) Biochim Biophys Acta 336:318–323
Sladić-Simić D, Kleinschmidt T, Braunitzer G (1977) Hoppe-Seyler's Z Physiol Chem 358:591–594
Steigemann W, Weber E (1979) J Mol Biol 127:309–338
Stensiö E (1958) Traité de Zoologie 13:173–425
Stenzel P, Brimhall B, Jones R, Black J, Mc Lachlan A, Gibson D (1979) J Biol Chem 254:2071–2076
Svedberg T, Eriksson-Quensel IB (1934) J Am Chem Soc 56:1700–1706
Takano T (1977) J Mol Biol 110:537–568
Tentori L, Vivaldi G, Carta S, Marinucci M, Massa A, Antonini E, Brunori M (1973) Int J Peptide Protein Res 5:187–200
Tucker PW, Phillips SEV, Perutz MF, Houtchens RA, Caughey WS (1978) In: Caughey WS (ed) Biochemical and Clinical Aspects of Hemoglobin Abnormalities. Academic Press, pp 1–15
Wald G, Riggs A (1951) J Gen Physiol 35:45–53
Zelenik M, Rudloff V, Braunitzer G (1979) Hoppe-Seyler's Z Physiol Chem 360:1879–1894
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Liljeqvist, G., Paléus, S. & Braunitzer, G. Hemoglobins, XLVIIII. J Mol Evol 18, 102–108 (1982). https://doi.org/10.1007/BF01810828
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DOI: https://doi.org/10.1007/BF01810828