In Rhodobacter sphaeroides Respiratory Nitrate Reductase, the Kinetics of Substrate Binding Favors Intramolecular Electron Transfer

Journal of the American Chemical Society

Volumn 126, Issue 5, 2004, Pages 1328-1329

  Frangioni, Bettina ^a   Arnoux, Pascal ^b   Sabaty, Monique ^b   Pignol, David ^b   Bertrand, Patrick ^a   Guigliarelli, Bruno ^a   Léger, Christophe ^a  

^a CNRS   (France)

^b IRFM   (France)

Author keywords

[No Author keywords available]

Indexed keywords

NITRATE REDUCTASE;

ARTICLE; BINDING KINETICS; CATALYSIS; CONCENTRATION RESPONSE; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; ENZYME SUBSTRATE COMPLEX; MICHAELIS CONSTANT; NONHUMAN; OXIDATION REDUCTION POTENTIAL; OXIDATION REDUCTION REACTION; POTENTIOMETRY; RHODOBACTER SPHAEROIDES;

ELECTROCHEMISTRY; ELECTRONS; KINETICS; NITRATE REDUCTASE; NITRATE REDUCTASES; OXIDATION-REDUCTION; RHODOBACTER SPHAEROIDES;

EID: 1042288190     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja0384072     Document Type: Article

References (23)

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10. 2) with 1 μL of 90 μM NapAB solution. Experiments were performed under a nitrogen atmosphere, with buffers consisting of either 5 mM in each of CHES, HEPES, MES, TAPS, NaAc and 0.1 M NaCl (Figure 1), or 50 mM TRIS and 0.1 M NaCl (Figure 2).
11. Notations: F, Faraday constant; R, gas constant; T, temperature; S, substrate concentration; A, electrode surface; Γ. electroactive coverage. The other symbols are defined in the text.
12. Léger, C.; Jones, A. K.; Albracht, S. P. J.; Armstrong, F. A. J. Phys. Chem. B 2002, 106, 13058-13063.
13. V ion naturally explains that no extrema in the activity should appear. Sulfite oxidases, which are not members of the DMSO reductase family, do not show complex electrochemical modulation of catalytic activity (Elliott, S. J.; McElhaney, A. E.; Feng, C.; Enemark, J. H.; Armstrong, F. A. J. Am. Chem. Soc. 2002, 124, 11612-11613. Aguey-Zinsou, K.-F.; Bernhardt, P. V.; Kappler, U.; McEwan, A. G. J. Am. Chem. Soc. 2003, 125, 530-535).
14. V ion naturally explains that no extrema in the activity should appear. Sulfite oxidases, which are not members of the DMSO reductase family, do not show complex electrochemical modulation of catalytic activity (Elliott, S. J.; McElhaney, A. E.; Feng, C.; Enemark, J. H.; Armstrong, F. A. J. Am. Chem. Soc. 2002, 124, 11612-11613. Aguey-Zinsou, K.-F.; Bernhardt, P. V.; Kappler, U.; McEwan, A. G. J. Am. Chem. Soc. 2003, 125, 530-535).
15. V ion naturally explains that no extrema in the activity should appear. Sulfite oxidases, which are not members of the DMSO reductase family, do not show complex electrochemical modulation of catalytic activity (Elliott, S. J.; McElhaney, A. E.; Feng, C.; Enemark, J. H.; Armstrong, F. A. J. Am. Chem. Soc. 2002, 124, 11612-11613. Aguey-Zinsou, K.-F.; Bernhardt, P. V.; Kappler, U.; McEwan, A. G. J. Am. Chem. Soc. 2003, 125, 530-535).
16. V ion naturally explains that no extrema in the activity should appear. Sulfite oxidases, which are not members of the DMSO reductase family, do not show complex electrochemical modulation of catalytic activity (Elliott, S. J.; McElhaney, A. E.; Feng, C.; Enemark, J. H.; Armstrong, F. A. J. Am. Chem. Soc. 2002, 124, 11612-11613. Aguey-Zinsou, K.-F.; Bernhardt, P. V.; Kappler, U.; McEwan, A. G. J. Am. Chem. Soc. 2003, 125, 530-535).
17. E. coli nitrate reductase exhibits extremely complex waveshapes (Figure 2 in ref 4c), which cannot be explained by the simple considerations presented here.
18. In model compounds relevant to the DMSO reductase family, reduction of oxide proceeds according to second order, irreversible kinetics, and the large, negative entropy of activation indicates an associative transition state involving considerable Mo-O(substrate) bond making (Lim, B. S.; Holm, R. H. J. Am. Chem. Soc. 2001, 123, 1920-1930), in accordance with density functional calculations (Webster, C. E.; Hall, M. B. J. Am. Chem. Soc. 2001, 123, 5820-5821). In Rb, capsulatus DMSO reductase, formation of the enzyme-substrate complex (as opposed to the subsequent, first-order catalytic step) is rate determining at low pH (Adams, B.; Smith, A. T.; Bailey, S.; McEwan, A. G.; Bray, R. C. Biochemistry 1999, 38, 8501-8511).
19. In model compounds relevant to the DMSO reductase family, reduction of oxide proceeds according to second order, irreversible kinetics, and the large, negative entropy of activation indicates an associative transition state involving considerable Mo-O(substrate) bond making (Lim, B. S.; Holm, R. H. J. Am. Chem. Soc. 2001, 123, 1920-1930), in accordance with density functional calculations (Webster, C. E.; Hall, M. B. J. Am. Chem. Soc. 2001, 123, 5820-5821). In Rb, capsulatus DMSO reductase, formation of the enzyme-substrate complex (as opposed to the subsequent, first-order catalytic step) is rate determining at low pH (Adams, B.; Smith, A. T.; Bailey, S.; McEwan, A. G.; Bray, R. C. Biochemistry 1999, 38, 8501-8511).
20. In model compounds relevant to the DMSO reductase family, reduction of oxide proceeds according to second order, irreversible kinetics, and the large, negative entropy of activation indicates an associative transition state involving considerable Mo-O(substrate) bond making (Lim, B. S.; Holm, R. H. J. Am. Chem. Soc. 2001, 123, 1920-1930), in accordance with density functional calculations (Webster, C. E.; Hall, M. B. J. Am. Chem. Soc. 2001, 123, 5820-5821). In Rb, capsulatus DMSO reductase, formation of the enzyme-substrate complex (as opposed to the subsequent, first-order catalytic step) is rate determining at low pH (Adams, B.; Smith, A. T.; Bailey, S.; McEwan, A. G.; Bray, R. C. Biochemistry 1999, 38, 8501-8511).
21. Page, C. C.; Moser, C. C.; Chen, X.; Dutton, P. L. Nature 1999, 402, 47-52.
22. The recently determined crystal structure of E. coli nitrate reductase revealed that a proximal [4Fe-4S] in NarG has previously escaped characterization (Bertero, M. G.; Rothery, A. R.; Palak, M.; Hou, C.; Lim, C.; Lim, D.; Blasco, F.; Weiner, J. H.; Strynadka, N. C. J. Nat. Struct. Biol. 2003, 10, 681-687). In E. coli DMSO reductase, an equivalent, yet unidentified, cluster may be present in DmsA (Rothery, R. A., private communication).
23. The recently determined crystal structure of E. coli nitrate reductase revealed that a proximal [4Fe-4S] in NarG has previously escaped characterization (Bertero, M. G.; Rothery, A. R.; Palak, M.; Hou, C.; Lim, C.; Lim, D.; Blasco, F.; Weiner, J. H.; Strynadka, N. C. J. Nat. Struct. Biol. 2003, 10, 681-687). In E. coli DMSO reductase, an equivalent, yet unidentified, cluster may be present in DmsA (Rothery, R. A., private communication).