TY - JOUR
T1 - Characterization of a carbon monoxide complex of reduced dopamine β-hydroxylase
T2 - Evidence for inequivalence of the Cu(I) centers
AU - Blackburn, Ninian J.
AU - Pettingill, Trudie M.
AU - Seagraves, Karen S.
AU - Shigeta, Ronald T.
N1 - Copyright:
Copyright 2007 Elsevier B.V., All rights reserved.
PY - 1990/9/15
Y1 - 1990/9/15
N2 - Ascorbate-reduced dopamine β-hydroxylase (DBH) is inhibited by CO in a competitive manner with respect to molecular O2. Measurement of the stoichiometry of CO binding indicates 0.50 CO bound per Cu(I), which provides the first evidence that the Cu(I) centers in the reduced enzyme are structurally inequivalent. FTIR spectroscopy has been used to detect an infrared absorption band characteristic of coordinated CO, with v(CO) = 2089 cm-1. Comparison of this frequency with those of other Cu(I)-carbonyls in both inorganic and protein systems suggests a coordination site with fewer or less basic ligands than the 3-histidine site of carbonmonoxy hemocyanin.
AB - Ascorbate-reduced dopamine β-hydroxylase (DBH) is inhibited by CO in a competitive manner with respect to molecular O2. Measurement of the stoichiometry of CO binding indicates 0.50 CO bound per Cu(I), which provides the first evidence that the Cu(I) centers in the reduced enzyme are structurally inequivalent. FTIR spectroscopy has been used to detect an infrared absorption band characteristic of coordinated CO, with v(CO) = 2089 cm-1. Comparison of this frequency with those of other Cu(I)-carbonyls in both inorganic and protein systems suggests a coordination site with fewer or less basic ligands than the 3-histidine site of carbonmonoxy hemocyanin.
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M3 - Article
C2 - 2394729
AN - SCOPUS:0025025585
SN - 0021-9258
VL - 265
SP - 15383
EP - 15386
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 26
ER -