Formation of super-reduced Chromatium high-potential iron--sulphur protein in aqueous solution by pulse radiolysis.

Content Provider	Semantic Scholar
Author	Butler, John K. Sykes, A. Geoffrey Buxton, George V. Harrington, Pip Wilkins, Richard G.
Copyright Year	1980
Abstract	Both the oxidized and reduced forms of Hipip (high-potential iron--sulphur protein) are reduced (approx. 30% yields) by eaq.- in a single-stage process, rate constants 1.7 x 10(10) and 1.8 x 10(10) M-1 . s-1 respectively, at 25 degrees C, pH 7.0 (5 mM-phosphate). Super-reduced Hipip, which is formed in the latter case, has a spectrum which closely resembles that of reduced ferredoxin, i.e. Fe4S4 (SR)4(3-) clusters. The spectrum is stable over 2 s periods investigated. Super-reduced Hipip is reoxidized with O2, rate constant 4.8 x 10(6) M-1 . s-1 at 25 degrees C.
Starting Page	1
Ending Page	3
Page Count	3
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://www.biochemj.org/content/ppbiochemj/189/3/641.full.pdf
PubMed reference number	7213348v1
Volume Number	189
Issue Number	3
Journal	The Biochemical journal
Language	English
Access Restriction	Open
Subject Keyword	Chromatium Ferredoxin Oxygen Pulse Radiolysis inorganic phosphate
Content Type	Text
Resource Type	Article