NDLI: Active Site of Cytochrome cbb 3 *

Content Provider	PubMed Central
Author	Rauhamäki, Virve Bloch, Dmitry A. Verkhovsky, Michael I. Wikström, Mårten
Abstract	Cytochrome cbb 3 is the most distant member of the heme-copper oxidase family still retaining the following major feature typical of these enzymes: reduction of molecular oxygen to water coupled to proton translocation across the membrane. The thermodynamic properties of the six redox centers, five hemes and a copper ion, in cytochrome cbb 3 from Rhodobacter sphaeroides were studied using optical and EPR spectroscopy. The low spin heme b in the catalytic subunit was shown to have the highest midpoint redox potential (Em ,7 +418 mV), whereas the three hemes c in the two other subunits titrated with apparent midpoint redox potentials of +351, +320, and +234 mV. The active site high spin heme b 3 has a very low potential (Em ,7 -59 mV) as opposed to the copper center (CuB), which has a high potential (Em ,7 +330 mV). The EPR spectrum of the ferric heme b 3 has rhombic symmetry. To explain the origins of the rhombicity, the Glu-383 residue located on the proximal side of heme b 3 was mutated to aspartate and to glutamine. The latter mutation caused a 10 nm blue shift in the optical reduced minus oxidized heme b 3 spectrum, and a dramatic change of the EPR signal toward more axial symmetry, whereas mutation to aspartate had far less severe consequences. These results strongly suggest that Glu-383 is involved in hydrogen bonding to the proximal His-405 ligand of heme b 3, a unique interaction among heme-copper oxidases.
Related Links	http://dx.doi.org/10.1074/jbc.m808839200
Ending Page	11308
Page Count	8
Starting Page	11301
File Format	PDF
ISSN	00219258
e-ISSN	1083351X
Journal	The Journal of Biological Chemistry
Issue Number	17
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2009-04-24
Access Restriction	Open
Rights Holder	American Society for Biochemistry and Molecular Biology
Subject Keyword	Cell Biology Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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