{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,10,21]],"date-time":"2023-10-21T11:40:26Z","timestamp":1697888426445},"reference-count":16,"publisher":"Wiley","issue":"7","license":[{"start":{"date-parts":[[2004,2,1]],"date-time":"2004-02-01T00:00:00Z","timestamp":1075593600000},"content-version":"vor","delay-in-days":7154,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biopolymers"],"published-print":{"date-parts":[[1984,7]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Interest in the thermodynamics of the iron\u2010binding site in hemoproteins has increased in recent years due to refinements in x\u2010ray crystallographic studies of hemoproteins [see Deathage, J. F., Lee, R. S., Anderson, C. M. &amp; Moffat, K. (1976) <jats:italic>J. Mol. Biol.<\/jats:italic> <jats:bold>104<\/jats:bold>, 687\u2013706; Heidner, E. J., Ladner, R. C. &amp; Perutz, M. F. (1976) <jats:italic>J. Mol. Biol.<\/jats:italic> <jats:bold>104<\/jats:bold>, 707\u2013722; Deathage, J. F., Lee, R. S. &amp; Moffat, K. (1976) <jats:italic>J. Mol. Biol.<\/jats:italic> <jats:bold>104<\/jats:bold>, 723\u2013728; Ladner, R. C., Heidner, E. J. &amp; Perutz, M. F. (1976) <jats:italic>J. Mol. Biol.<\/jats:italic> <jats:bold>114<\/jats:bold>, 385\u2013414; Fermi, G. &amp; Perutz, M. F. (1977) <jats:italic>J. Mol. Biol.<\/jats:italic> <jats:bold>114<\/jats:bold>, 421\u2013431; Takano, T. (1977) <jats:italic>J. Mol. Biol.<\/jats:italic> <jats:bold>110<\/jats:bold>, 537\u2013568 and 569\u2013589], the synthesis and x\u2010ray analysis of model heme compounds [see Scheidt, W. R. (1977) <jats:italic>Acc. Chem. Res.<\/jats:italic> <jats:bold>10<\/jats:bold>, 339\u2013345; Kastner, M. E., Scheidt, W. R., Mashino, T. &amp; Reed, C. A. (1978) <jats:italic>J. Am. Chem. Soc.<\/jats:italic> <jats:bold>100<\/jats:bold>, 666\u2013667; Mashiko, T., Kastner, M. E., Spartalian, K., Scheidt, W. R. &amp; Reed, C. A. (1978) <jats:italic>J. Am. Chem. Soc.<\/jats:italic> <jats:bold>100<\/jats:bold>, 6354\u20136362; Hill, H. A. O., Skite, P. P., Buchler, J. W., Luchr, H., Tonn, M., Gregson, A. K. &amp; Pellizer, G. (1979) <jats:italic>Chem. Commun.<\/jats:italic> <jats:bold>4<\/jats:bold>, 151\u2013152; and Scheidt, W. R., Cohen, I. A. &amp; Kastner, M. E. (1979) <jats:italic>Biochemistry<\/jats:italic> <jats:bold>18<\/jats:bold>, 3546\u20133556], and the numerous data on heme\u2013protein interactions that account for the differences observed in ligand binding between the various species of animals. Numerous probes have been used and provide information about the structure and thermodynamics of the binding site, but no single probe can provide the complete picture [see Iizuka, T. &amp; Yonetani, T. (1970) <jats:italic>Adv. Biophys.<\/jats:italic> <jats:bold>1<\/jats:bold>, 157\u2013182; Smith, D. W. &amp; Williams, R. J. P. (1970) <jats:italic>Struct. Bond.<\/jats:italic> <jats:bold>7<\/jats:bold>, 1\u201345; and Spiro, T. G. (1975) <jats:italic>Biochim. Biophys. Acta<\/jats:italic> <jats:bold>416<\/jats:bold>, 169\u2013189].<\/jats:p>","DOI":"10.1002\/bip.360230702","type":"journal-article","created":{"date-parts":[[2004,12,30]],"date-time":"2004-12-30T01:33:53Z","timestamp":1104370433000},"page":"1147-1167","source":"Crossref","is-referenced-by-count":1,"title":["Analysis of the high\u2010 and low\u2010spin soret bands of horse\u2010heart metmyoglobin complexes"],"prefix":"10.1002","volume":"23","author":[{"given":"A. C. 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