2EIL: Cadmium Ion Binding Structure Of Bovine Heart Cytochrome C Oxidase In The Fully Oxidized State

Citation:
Abstract
Cytochrome c oxidase transfers electrons and protons for dioxygen reduction coupled with proton pumping. These electron and proton transfers are tightly coupled with each other for the effective energy transduction by various unknown mechanisms. Here, we report a coupling mechanism by a histidine (His-503) at the entrance of a proton transfer pathway to the dioxygen reduction site (D-pathway) of bovine heart cytochrome c oxidase. In the reduced state, a water molecule is fixed by hydrogen bonds between His-503 and Asp-91 of the D-pathway and is linked via two water arrays extending to the molecular surface. The microenvironment of Asp-91 appears in the x-ray structure to have a proton affinity as high as that of His-503. Thus, Asp-91 and His-503 cooperatively trap, on the fixed water molecule, the proton that is transferred through the water arrays from the molecular surface. On oxidation, the His-503 imidazole plane rotates by 180 degrees to break the hydrogen bond to the protonated water and releases the proton to Asp-91. On reduction, Asp-91 donates the proton to the dioxygen reduction site through the D-pathway. The proton collection controlled by His-503 was confirmed by partial electron transfer inhibition by binding of Zn2+ and Cd2+ to His-503 in the x-ray structures. The estimated Kd for Zn2+ binding to His-503 in the x-ray structure is consistent with the reported Kd for complete proton-pumping inhibition by Zn2+ [Kannt A, Ostermann T, Muller H, Ruitenberg M (2001) FEBS Lett 503:142-146]. These results suggest that His-503 couples the proton transfer for dioxygen reduction with the proton pumping.
PDB ID: 2EILDownload
MMDB ID: 46119
PDB Deposition Date: 2007/3/13
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.1  Å
Source Organism:
Similar Structures:
Biological Unit for 2EIL: 26-meric; determined by author and by software (PISA,PQS)
Molecular Components in 2EIL
Label Count Molecule
Proteins (26 molecules)
2
Cytochrome C Oxidase Subunit 1
Molecule annotation
2
Cytochrome C Oxidase Subunit 2(Gene symbol: COX2)
Molecule annotation
2
Cytochrome C Oxidase Subunit 3
Molecule annotation
2
Cytochrome C Oxidase Subunit 4 Isoform 1(Gene symbol: COX4I1)
Molecule annotation
2
Cytochrome C Oxidase Polypeptide VA(Gene symbol: COX5A)
Molecule annotation
2
Cytochrome C Oxidase Polypeptide VB(Gene symbol: COX5B)
Molecule annotation
2
Cytochrome C Oxidase Polypeptide Via-heart(Gene symbol: COX6A2)
Molecule annotation
2
Cytochrome C Oxidase Subunit VIB Isoform 1(Gene symbol: COX6B1)
Molecule annotation
2
Cytochrome C Oxidase Polypeptide VIC(Gene symbol: MGC148714)
Molecule annotation
2
Cytochrome C Oxidase Polypeptide Viia-heart(Gene symbol: COX7A1)
Molecule annotation
2
Cytochrome C Oxidase Polypeptide Viib(Gene symbol: COX7B)
Molecule annotation
2
Cytochrome C Oxidase Polypeptide Viic(Gene symbol: COX7C)
Molecule annotation
2
Cytochrome C Oxidase Polypeptide Viii-heart(Gene symbol: COX8B)
Molecule annotation
Chemicals (55 molecules)
1
2
2
2
3
2
4
3
5
4
6
6
7
8
8
2
9
2
10
8
11
4
12
6
13
4
14
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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