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.
Full text
PDF



Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Adman E., Watenpaugh K. D., Jensen L. H. NH---S hydrogen bonds in Peptococcus aerogenes ferredoxin, Clostridium pasteurianum rubredoxin, and Chromatium high potential iron protein. Proc Natl Acad Sci U S A. 1975 Dec;72(12):4854–4858. doi: 10.1073/pnas.72.12.4854. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Butler J., Henderson R. A., Armstrong F. A., Sykes A. G. Mechanism of formation, spectrum and reactivity of half-reduced eight-iron Clostridium pasteurianum ferredoxin in pulse-radiolysis studies and the non-co-operativity of the four-iron clusters. Biochem J. 1979 Nov 1;183(2):471–474. doi: 10.1042/bj1830471. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cammack R. "Super-reduction" of chromatium high-potential iron-sulphur protein in the presence of dimethyl sulphoxide. Biochem Biophys Res Commun. 1973 Sep 18;54(2):548–554. doi: 10.1016/0006-291x(73)91457-5. [DOI] [PubMed] [Google Scholar]
- Dus K., De Klerk H., Sletten K., Bartsch R. G. Chemical characterization of high potential iron proteins from Chromatium and Rhodopseudomonas gelatinosa. Biochim Biophys Acta. 1967 Jun 27;140(2):291–311. doi: 10.1016/0005-2795(67)90470-9. [DOI] [PubMed] [Google Scholar]
- Dus K., Tedro S., Bartsch R. G. The complete amino acid sequence of Chromatium high potential iron sulfur protein. J Biol Chem. 1973 Nov 10;248(21):7318–7331. [PubMed] [Google Scholar]
- Faraggi M., Tal Y. The reaction of the hydrated electron with amino acids, peptides, and proteins in aqueous solution. II. Formation of radicals and electron transfer reactions. Radiat Res. 1975 May;62(2):347–356. [PubMed] [Google Scholar]
- Hong J. S., Rabinowitz J. C. Molar extinction coefficient and iron and sulfide content of clostridial ferredoxin. J Biol Chem. 1970 Oct 10;245(19):4982–4987. [PubMed] [Google Scholar]
- Mayhew S. G., Petering D., Palmer G., Foust G. P. Spectrophotometric titration of ferredoxins and Chromatium high potential iron protein with sodium dithionite. J Biol Chem. 1969 Jun 10;244(11):2830–2834. [PubMed] [Google Scholar]
- Stombaugh N. A., Sundquist J. E., Burris R. H., Orme-Johnson W. H. Oxidation-reduction properties of several low potential iron-sulfur proteins and of methylviologen. Biochemistry. 1976 Jun 15;15(12):2633–2641. doi: 10.1021/bi00657a024. [DOI] [PubMed] [Google Scholar]
- de Kok J., Butler J., Braams R., van Gelder B. F. The reduction of porphyrin cytochrome c by hydrated electrons and the subsequent electron transfer reaction from reduced porphyrin cytochrome c to ferricytochrome c. Biochim Biophys Acta. 1977 May 11;460(2):290–298. doi: 10.1016/0005-2728(77)90215-8. [DOI] [PubMed] [Google Scholar]
