The energy-transducing nicotinamide transhydrogenases (THs) of mammalian and bacteria are structurally related membrane-bound enzymes that catalyze the direct transfer of a hydride ion between NAD(H) and NADP(H) in a reaction coupled to transmembrane proton translocation. The NADPH produced by TH is to reduce H2O2, which is capable of causing oxidative damage to intramitochondrial DNA and proteins, and initiating lipid peroxidation. Therefore, in order to understand the proton translocation mechanism and the reaction catalyzed by these enzymes a detailed knowledge of their three dimensional structure is essential. Weakly diffracting, highly anisotropic and radiation sensitve crystals of the alfa-1 subunit of R. rubrum TH have been obtained. These crystals diifract only to 4 E resolution using in-house x-ray source, whereas, the same crystals diffract to 2.7 E on BL7-1.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-20
Application #
6119483
Study Section
Project Start
1999-03-01
Project End
2000-04-14
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
20
Fiscal Year
1999
Total Cost
Indirect Cost
Name
Stanford University
Department
Type
DUNS #
800771545
City
Stanford
State
CA
Country
United States
Zip Code
94305
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