The MoFe protein of nitrogenase is under intense study as the catalytic component of the biological N2 fixation system. We are using x-ray absorption spectroscopic examination of the Mo site of its Mo-Fe-S cluster active site, both in the intact enzyme and in its isolated form (called FeMoco). These experiments have so far been limited to wild-type enzyme. Recently, we have been able to obtain large quantities of altered forms of the MoFe protein from mutant organisms and have also obtained altered forms of FeMoco. EXAFS analysis of these species should define both the portions of FeMoco that are required for biological activity and the transformation that occurs at the Mo site during FeMoco biosynthesis. We are further studying the effects of substrates and inhibitor on the structure of the active site.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
3P41RR001209-23S1
Application #
6658765
Study Section
Project Start
2002-03-01
Project End
2003-02-28
Budget Start
Budget End
Support Year
23
Fiscal Year
2002
Total Cost
$143,176
Indirect Cost
Name
Stanford University
Department
Type
DUNS #
800771545
City
Stanford
State
CA
Country
United States
Zip Code
94305
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