Conformational distribution in protein-bound [3Fe-4S]+ clusters: CW and pulsed EPR and iron-57 ENDOR of D. gigas hydrogenase

Autor:	Andrew L. P. Houseman, Brian M. Hoffman, Chaoliang Fan, Peter E. Doan
Rok vydání:	1993
Předmět:	Hydrogenase Chemistry Pulsed EPR General Engineering Analytical chemistry Spectral line law.invention Crystallography Protein structure law Cluster (physics) Desulfovibrio gigas Tensor Physical and Theoretical Chemistry Electron paramagnetic resonance
Zdroj:	The Journal of Physical Chemistry. 97:3017-3021
ISSN:	1541-5740 0022-3654
DOI:	10.1021/j100114a031
Popis:	This paper discusses 9- and 35-GHz EPR spectra of the Desulfovibrio gigas [3Fe-4S] + cluster and also describes 35-GHz CW 57 Fe ENDOR measurements of isotopically enriched protein. The EPR spectra of [3Fe-4S] + clusters typically cannot be described by a well-defined g tensor. Their properties instead can be modeled with a formal treatment that assumes there is a distribution in the g values. This treatment implicitly assumes that the EPR spectra of such clusters are controlled by a distribution in protein conformation and cluster structure, but the validity of this assumption has never been confirmed by an experiment that correlates the EPR spectrum of a cluster with a microscopy cluster property
Databáze:	OpenAIRE
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