Crystallographic Studies of Xe And Kr Binding Within the Large Internal Cavity of Cytochrome Ba(3) From Thermus Thermophilus: Structural Analysis And Role of Oxygen Transport Channels in the Heme-Cu Oxidases

Cytochrome ba{sub 3} is a cytochrome c oxidase from the plasma membrane of Thermus thermophilus and is the preferred terminal enzyme of cellular respiration at low dioxygen tensions. Using cytochrome ba{sub 3} crystals pressurized at varying conditions under Xe or Kr gas, and X-ray data for six crys...

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Bibliographic Details
Published in:Biochemistry (Easton) 2009-05, Vol.47 (16)
Main Authors: Luna, V.M., Chen, Y., Fee, J.A., Stout, C.D.
Format: Article
Language:English
Subjects:
AFFINITY
ATOMS
BASIC BIOLOGICAL SCIENCES
BIFURCATION
CRYSTALS
CYTOCHROMES
DATA
DIFFUSION
ENZYMES
GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE
HOLES
JOINTS
LENGTH
MEMBRANES
ORIENTATION
Other,CHEM, BIO
OXIDASES
OXYGEN
PARTICLE TRACKS
PLASMA
PROTEINS
RESIDUES
RESPIRATION
SURFACES
TRANSPORT
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Summary:Cytochrome ba{sub 3} is a cytochrome c oxidase from the plasma membrane of Thermus thermophilus and is the preferred terminal enzyme of cellular respiration at low dioxygen tensions. Using cytochrome ba{sub 3} crystals pressurized at varying conditions under Xe or Kr gas, and X-ray data for six crystals, we identify the relative affinities of Xe and Kr atoms for as many as seven distinct binding sites. These sites track a continuous, Y-shaped channel, 18--20 {angstrom} in length, lined by hydrophobic residues, which leads from the surface of the protein where two entrance holes, representing the top of the Y, connect the bilayer to the {alpha}{sub 3}-Cu{sub B} center at the base of the Y. Considering the increased affinity of O{sub 2} for hydrophobic environments, the hydrophobic nature of the channel, its orientation within the bilayer, its connection to the active site, its uniform diameter, its virtually complete occupation by Xe, and its isomorphous presence in the native enzyme, we infer that the channel is a diffusion pathway for O{sub 2} into the dinuclear center of cytochrome ba{sub 3}. These observations provide a basis for analyzing similar channels in other oxidases of known structure, and these structures are discussed in terms of mechanisms of O{sub 2} transport in biological systems, details of CO binding to and egress from the dinuclear center, the bifurcation of the oxygen-in and water-out pathways, and the possible role of the oxygen channel in aerobic thermophily.
ISSN:0006-2960
1520-4995