CopC protein from Pseudomonas syringae: Intermolecular transfer of copper from both the copper(I) and copper(II) sites

Inorganic Chemistry

Volumn 44, Issue 15, 2005, Pages 5203-5205

  Koay, Melissa ^a   Zhang, Lianyi ^a   Yang, Binsheng ^c   Maher, Megan J ^b   Xiao, Zhiguang ^a   Wedd, Anthony G ^a  

^a UNIVERSITY OF MELBOURNE   (Australia)

^b UNIVERSITY OF SYDNEY   (Australia)

^c SHANXI UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; COPC PROTEIN, BACTERIA; COPPER;

ARTICLE; CHEMISTRY; METABOLISM; OXIDATION REDUCTION REACTION; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PSEUDOMONAS SYRINGAE; THERMODYNAMICS;

BACTERIAL PROTEINS; COPPER; OXIDATION-REDUCTION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PSEUDOMONAS SYRINGAE; THERMODYNAMICS;

EID: 23244449071     PISSN: 00201669     EISSN: None     Source Type: Journal    
DOI: 10.1021/ic0506198     Document Type: Article

References (14)

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10. II form generated under the conditions of Figure 1.
11. D can be derived because these experiments are at the limit of detection: less than 1 % of protein binds Cu at equilibrium.
12. II) (Table S2 of the Supporting Information).
13. K for reaction 4 was assessed from the relative integrated peak area of each component of the elution profile (part g) of the figure.
14. The identity of each protein component isolated from the elution profiles of Figure 2 was confirmed by ESI-MS and the copper content (Table S3 of the Supporting Information). apo-H1F □⊄ showed little affinity for the Mono-S resin at pH 7, eluting as a broad band of variable position close to the start of the NaCl gradient. That position depended markedly on the ionic strength and sample volume.