Abstract:
:The effects of structural modifications of the flavin mononucleotide (FMN) prosthetic group of Clostridium pasteurianum flavodoxin on the kinetics of electron transfer to the oxidized form (from 5-deazariboflavin semiquinone produced by laser flash photolysis) and from the semiquinone form (to horse heart cytochrome c by using stopped-flow spectrophotometry) have been investigated. The analogues used were 7,8-dichloro-FMN, 8-chloro-FMN, 7-chloro-FMN, and 5,6,7,8-tetrahydro-FMN. The ionic strength dependence of cytochrome c reduction was not affected by chlorine substitution, although the specific rate constants for complex formation and decay were appreciably smaller. On the other hand, all of the chlorine analogues had the same rate constant for deazariboflavin semiquinone oxidation. The rate constants for tetrahydro-FMN flavodoxin semiquinone reduction of cytochrome c were considerably smaller than those for the native protein. The implications of these results for the electron-transfer mechanism of flavodoxin are discussed.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Simondsen RP,Tollin Gdoi
10.1021/bi00281a034subject
Has Abstractpub_date
1983-06-07 00:00:00pages
3008-16issue
12eissn
0006-2960issn
1520-4995journal_volume
22pub_type
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