Insights into the functional role of the tyrosine-histidine linkage in cytochrome c oxidase [17]

Journal of the American Chemical Society

Volumn 122, Issue 10, 2000, Pages 2403-2404

  McCauley, Kevin M ^a   Vrtis, Jennifer M ^a   Dupont, Joseph ^a   Van Der Donk, Wilfred A ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C OXIDASE; HISTIDINE; TYROSINE;

CATALYSIS; CHEMICAL BINDING; CROSS LINKING; ENZYME ACTIVE SITE; ENZYME ANALYSIS; LETTER; OXIDATION REDUCTION POTENTIAL; PROTEIN BINDING; PROTEIN MODIFICATION;

EID: 0034654622     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja993774s     Document Type: Letter

References (26)

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10. 2b An alternative view of proton movement is presented in refs 2c,d.
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12. a values were determined by two independent titrations of 0.4 mM analyte using 17 different buffer solutions adjusted to 0.3 M ionic strength with KCl.
13. a of the phenol by resonance stabilization of the conjugate anion. The increased acidity of the phenol is therefore best explained as an inductive electron-withdrawing effect. The influence of copper coordination will depend on its oxidation state as well as coordination geometry. Generally, coordination will increase the inductive electron-withdrawing effect, but dπ-pπ back-bonding may offset this. Note also that the cross-link lowers the basicity of the imidazole nitrogen, which will weaken its coordinating ability.
14. -1, 1 showed a peak potential 73.0 ±4.9 mV more positive than p-cresol.
15. Two independent determinations of the pH dependence of the half-wave potential both showed a significantly better fit to three than to two dissociation constants. Figures showing alternative fits are provided in the Supporting Information.
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24. 2+ via the direct covalent connection (Figure 1).
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