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Resonance Raman spectroscopic study on the iron—sulfur proteins containing [2Fe—2S] clusters
Author(s) -
Ozaki Yukihiro,
Nagayama Kuniaki,
Kyogoku Yoshimasa,
Hase Toshiharu,
Matsubara Hiroshi
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80387-1
Subject(s) - raman spectroscopy , resonance (particle physics) , chemistry , sulfur , cysteine , crystallography , spectral line , nuclear magnetic resonance , biochemistry , organic chemistry , atomic physics , physics , optics , astronomy , enzyme
Resonance Raman spectra have been obtained for Spinacea oleracea, Phytolacca americana and Halobacterium halobium ferrodoxins. These spectra were very similar to each other in terms of both vibrational frequencies and relative intensities, strongly suggesting that their molecular structures of active centers are very similar. The resonance Raman spectra were, however, fairly different in the frequencies of Fe—S(Cys) stretching modes from the spectrum of beef adrenodoxin previously reported. Probably the nature of Fe—S(Cys)‐bonding and/or the manner of cysteine ligation is somewhat different between adrenodoxin and the other [2Fe—2S] ferrodoxins.