Resonance Raman excitation profiles indicate multiple Cys .fwdarw. Cu charge transfer transitions in type 1 copper proteins

Autor:	Thomas M. Loehr, Joann Sanders-Loehr, Joan Selverstone Valentine, Jane Han, B. A. Averill, Yi Lu
Rok vydání:	1993
Předmět:	Copper protein Chemistry Analytical chemistry General Chemistry Dihedral angle Chromophore Resonance (chemistry) Biochemistry Catalysis Bond length Crystallography symbols.namesake Colloid and Surface Chemistry Absorption band symbols Moiety Raman spectroscopy
Zdroj:	Journal of the American Chemical Society. 115:4256-4263
ISSN:	1520-5126 0002-7863
DOI:	10.1021/ja00063a048
Popis:	Nitrite reductase (NiR) from Achromobacrer cycloclastes and mutant yeast Cu-Zn superoxide dismutase (with Cys substituted for His80 and Cu for Zn) have both been shown to contain type 1 Cu sites. However, they differ from other type 1 (blue) Cu proteins in that they are green: the absorption band at ∼460 nm is more intense than the one at ∼600 nm. Excitation within either of these absorption bands leads to resonance Raman (RR) spectra that are characteristic of type 1 Cu with a large number of peaks between 250 and 500 cm -1 . The RR spectra of NiR and mutant SOD are thus indicative of a Cu-cysteinate chromophore with a short Cu-S bond distance (∼2.1 A) and a coplanar cysteine moiety (Cu-S γ -C β -C α dihedral angle ∼180 o )
Databáze:	OpenAIRE
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