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Evidence for a copper‐coordinated histidine–tyrosine cross‐link in the active site of cytochrome oxidase
Author(s) -
Buse Gerhard,
Soulimane Tewfik,
Dewor Manfred,
Meyer Helmut E.,
Blüggel Martin
Publication year - 1999
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.8.5.985
Subject(s) - histidine , cytochrome c oxidase , chemistry , active site , tyrosine , copper , biochemistry , cytochrome , enzyme , organic chemistry
Abstract Following hints from X‐ray data (Ostermeier C et al., 1997, Proc Natl Acad Sci USA 94 :10547–10553; Yoshikawa S et al., 1998, Science 280 :1723–1729), chemical evidence is presented from four distantly related cytochrome‐ c oxidases for the existence of a copper B ‐coordinated His240–Tyr244) cross‐link at the O 2 ‐activating Heme Fea 3 –Cu B center in the catalytic subunit I of the enzyme. The early evolutionary invention of this unusual structure may have prevented demaging OH‐radical release at e – ‐transfer to dioxygen and thus have enabled O 2 respiration.