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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
27
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pubmed:dateCreated |
1986-4-7
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pubmed:abstractText |
The structures of photoactivated carboxymyoglobin (Mb*CO) at temperatures to 10 K have been investigated by Fourier transform infrared (FT-IR) spectroscopy, visible spectroscopy, and near-infrared spectroscopy. Two energy states for *CO are observed by FT-IR, which are altered in frequency by 94% and 88% of the difference from the ground-state heme CO toward free CO gas [Alben, J. O., Beece, D., Bowne, S. F., Doster, W., Eisenstein, L. Frauenfelder, H., Good, D., McDonald, J. D., Marden, M. C., Moh, P. P., Reinisch, L., Reynolds, A. H., Shyamsundar, E., & Yue, K. T. (1982) Proc. Natl. Acad. Sci. U.S.A. 79, 3744-3748]. Ground-state MbCO shows no absorption in the near-infrared from 700 to 1200 nm. Conversely, Mb*CO shows an absorption near 766 nm, similar to that of ferrous myoglobin (deoxy-Mb) at 758 nm. These data are compared with Mössbauer isomer shifts and quadrupole splitting [Spartalian, K., Lang, G., & Yonetani, T. (1976) Biochim. Biophys. Acta 428, 281-290] and magnetic susceptibility measurements [Roder, H., Berendzen, J., Bowne, S. F., Frauenfelder, H., Sauke, T. B., Shyamsunder, E., & Weissman, M. B. (1984) Proc. Natl. Acad. Sci. U.S.A. 81, 2359-2363], which clearly indicate that the iron in both Mb*CO and deoxy-Mb is in the high-spin Fe(II) state, as does the heme transition in the Soret [Iizuka, T., Yamamoto, H., Kotani, M., & Yonetani, T. (1974) Biochim. Biophys. Acta 371, 126-139]. Thus the electronic structure of iron in Mb*CO is nearly identical with that of deoxy-Mb, and *CO is only slightly perturbed from the free gas.(ABSTRACT TRUNCATED AT 250 WORDS)
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
31
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pubmed:volume |
24
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7964-70
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:4092047-Animals,
pubmed-meshheading:4092047-Fourier Analysis,
pubmed-meshheading:4092047-Models, Molecular,
pubmed-meshheading:4092047-Muscles,
pubmed-meshheading:4092047-Myoglobin,
pubmed-meshheading:4092047-Photolysis,
pubmed-meshheading:4092047-Protein Conformation,
pubmed-meshheading:4092047-Spectrophotometry,
pubmed-meshheading:4092047-Spectrum Analysis,
pubmed-meshheading:4092047-Whales
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pubmed:year |
1985
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pubmed:articleTitle |
Structures of photolyzed carboxymyoglobin.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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