Literature DB >> 3689779

The effect of ethylenediamine chemical modification of plastocyanin on the rate of cytochrome f oxidation and P-700+ reduction.

G P Anderson1, D G Sanderson, C H Lee, S Durell, L B Anderson, E L Gross.   

Abstract

Chemical modification of plastocyanin was carried out using ethylenediamine plus a water-soluble carbodiimide, which has the effect of replacing a negatively charged carboxylate group with a positively charged amino group at pH 6-8. The conditions were adjusted to produce a series of singly and doubly modified forms of plastocyanin. Differences in charge configuration allowed separation of these forms on a Pharmacia fast protein liquid chromatograph using a Mono Q anion exchange column. These forms were used to study the interaction of plastocyanin with its reaction partner cytochrome f. The rate of cytochrome f oxidation was progressively inhibited upon incorporation of increasing numbers of ethylenediamine moieties indicating a positively charged binding site on cytochrome f. However, differential inhibition was obtained for the various singly modified forms allowing mapping of the binding site on plastocyanin. The greatest inhibition was found for forms modified at negatively charged residues Nos. 42-45 and Nos. 59-61 which comprise a negative patch surrounding Tyr-83. In contrast, the form modified at residue No. 68, on the opposite side of the globular plastocyanin molecule, showed the least inhibition. It can be concluded that the binding site for cytochrome f is located in the vicinity of residues Nos. 42-45 and Nos. 59-61. Modification of plastocyanin at residues Nos. 42-45 showed no effect on the rate of P-700+ reduction, suggesting that these residues are not involved in the binding of Photosystem I. However, an increase in the rate of P-700+ reduction was observed for plastocyanins modified at residue No. 68 or Nos. 59-61, which is consistent with the idea that the reaction domain of Photosystem I is negatively charged and Photosystem I binds at the top of the molecule and accepts electrons via His-87 in plastocyanin. These results raise the possibility that plastocyanin can bind both cytochrome f and Photosystem I simultaneously. The effect of ethylenediamine modification on the formal potential of plastocyanin was also examined. The formal potential of control plastocyanin was found to be +372 +/- 5 mV vs. normal hydrogen electrode at pH 7. All modified forms showed a positive shift in formal potential. Singly modified forms showed increases in formal potentials between +8 and +18 mV with the largest increases being observed for plastocyanins modified at residues Nos. 42-45 or Nos. 59-61.

Entities:  

Mesh:

Substances:

Year:  1987        PMID: 3689779     DOI: 10.1016/0005-2728(87)90117-4

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  20 in total

1.  Surface interactions in the complex between cytochrome f and the E43Q/D44N and E59K/E60Q plastocyanin double mutants as determined by (1)H-NMR chemical shift analysis.

Authors:  A Bergkvist; M Ejdebäck; M Ubbink; B G Karlsson
Journal:  Protein Sci       Date:  2001-12       Impact factor: 6.725

2.  The interaction of methanol dehydrogenase and cytochrome cL in the acidophilic methylotroph Acetobacter methanolicus.

Authors:  H T Chan; C Anthony
Journal:  Biochem J       Date:  1991-11-15       Impact factor: 3.857

3.  A Brownian Dynamics computational study of the interaction of spinach plastocyanin with turnip cytochrome f: the importance of plastocyanin conformational changes.

Authors:  Elizabeth L Gross
Journal:  Photosynth Res       Date:  2007-10-31       Impact factor: 3.573

4.  Brownian dynamics simulations of the interaction of Chlamydomonas cytochrome f with plastocyanin and cytochrome c6.

Authors:  Elizabeth L Gross; Douglas C Pearson
Journal:  Biophys J       Date:  2003-09       Impact factor: 4.033

5.  Plastocyanin: Structure and function.

Authors:  E L Gross
Journal:  Photosynth Res       Date:  1993-08       Impact factor: 3.573

6.  Brownian dynamics study of the interaction between plastocyanin and cytochrome f.

Authors:  D C Pearson; E L Gross
Journal:  Biophys J       Date:  1998-12       Impact factor: 4.033

7.  Electrostatic properties of cytochrome f: implications for docking with plastocyanin.

Authors:  D C Pearson; E L Gross; E S David
Journal:  Biophys J       Date:  1996-07       Impact factor: 4.033

8.  Cytochrome f: Structure, function and biosynthesis.

Authors:  J C Gray
Journal:  Photosynth Res       Date:  1992-12       Impact factor: 3.573

9.  De novo design and characterization of copper metallopeptides inspired by native cupredoxins.

Authors:  Jefferson S Plegaria; Matteo Duca; Cédric Tard; Thomas J Friedlander; Aniruddha Deb; James E Penner-Hahn; Vincent L Pecoraro
Journal:  Inorg Chem       Date:  2015-09-18       Impact factor: 5.165

10.  Chloroplast thylakoid proteins associated with sequestered proton-buffering domains. Plastocyanin contributes buffering groups to localized proton domains.

Authors:  F C Allnutt; E Atta-Asafo-Adjei; R A Dilley
Journal:  J Bioenerg Biomembr       Date:  1989-08       Impact factor: 2.945

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.