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STRUCTURAL-CHANGES ...
STRUCTURAL-CHANGES IN THE WATER-OXIDIZING COMPLEX MONITORED VIA THE PH-DEPENDENCE OF THE REDUCTION RATE OF REDOX STATE S-1 BY HYDRAZINE AND HYDROXYLAMINE IN ISOLATED SPINACH THYLAKOIDS
- Article/chapterEnglish1995
Publisher, publication year, extent ...
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2002-05-01
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AMER CHEMICAL SOC,1995
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printrdacarrier
Numbers
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LIBRIS-ID:oai:DiVA.org:uu-514208
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https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-514208URI
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https://doi.org/10.1021/bi00018a021DOI
Supplementary language notes
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Language:English
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Summary in:English
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Subject category:ref swepub-contenttype
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Subject category:art swepub-publicationtype
Notes
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A detailed kinetic analysis is presented for the pH dependence of the reduction of the water-oxidizing complex (WOC) in redox state S-1 by hydrophilic amines NH(2)R (R = NH2, OH) in suspensions of isolated thylakoids. Measurements of patterns of the oxygen yield induced by a train of single-turnover flashes and evaluation of the data within the framework of an extended Kok model [Messinger, J., Wacker, U., and Renger, G. (1991) Biochemistry 30, 7852-7862] led to the following results: (a) the rate constants k(s1)(NH(2)R) exhibit strikingly similar pH dependencies for NH2OH and NH2NH2 with ''titration waves'' at pH 5.3-5.6; 6.2-6.5, and above a critical pH value of about 7.4; (b) the differences in the reaction mechanism between NH2OH (1-electron reduction) and NH2NH2 (2-electron reduction) are almost pH-independent; (c) the ratio of the rate constants, k(s1)(NH2OH)/k(s1)(NH2NH2), decreases by a factor of about 9 within the range 5 < pH < 8.5. A detailed analysis reveals that these data cannot be consistently explained by the assumption that the unprotonated forms NH2OH and NH2NH2 are the active species while the protonated cations [NH3OH](+) and [N2H5](+) are nonreactive. A quantitative description is achieved by the additional postulate that pH-dependent structural changes take place in the WOC, thereby modulating the reactivity toward exogenous redox active amines of the type NH(2)R. On the basis of the results of this study and a recent report [Messinger, J., and Renger, G. (1994) Biochemistry 33, 10896-10905], it is inferred that the WOC undergoes three specific structural changes, with characteristic pH values of 5.3-5.5,6.2-6.5, and above 7.4.
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Messinger, Johannes,1963-Max Volmer Institut für Biophysikalische und Physikalische Chemie, Technischen Universität, Berlin, Germany(Swepub:uu)johme269
(author)
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RENGER, G
(author)
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Max Volmer Institut für Biophysikalische und Physikalische Chemie, Technischen Universität, Berlin, Germany
(creator_code:org_t)
Related titles
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In:Biochemistry: AMER CHEMICAL SOC34:18, s. 6175-61820006-29601520-4995
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