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MO Study of flavin–protein interactions in flavodoxin catalysis

✍ Scribed by Murray F. Teitell; J. Lawrence Fox

Publisher
John Wiley and Sons
Year
1980
Tongue
English
Weight
301 KB
Volume
18
Category
Article
ISSN
0020-7608

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✦ Synopsis

Abstract

MINDO/3 calculations have been performed on the Clostridium MP flavodoxin active site (a complex of the redox active coenzyme flavin mononucleotide sandwiched between the side chains of methionine and tryptophan) at various redox levels using coordinates derived from x‐ray diffraction studies of the holoenzyme. Frontier orbital indices were calculated and indicate that reduction of the flavin is accompanied by induced polar states in the amino acid side chains. This stabilization of charge by the amino acid side chains could account for the reaction rate enhancement of flavin reduction catalyzed by flavodoxin. Frontier orbitals for free flavin, for the flavodoxin bound flavin without the amino acid side chains, and for the oxidized Desulfovibrio vulgaris flavodoxin active site were computed for comparison.

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