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Virginia Tech

Characterization of an altered MoFe protein from a nifV- strain from Azotobacter vinelandii

Abstract

dc:description.abstract

The site of substrate binding and reduction for the nitrogenase complex is located on the iron molybdenum cofactor (FeMo-co) which is contained within the a-subunit of the molybdenum iron protein. FeMo co consists of a metal sulfur core composed of an FeS cluster bridged by three inorganic sulfides to a MoFeS cluster. An organic acid, homocitrate, is coordinated to the Mo atom through its 2-carboxy and 2-hydroxy groups. Homocitrate is formed by the condensation of acetyl-CoA and a-ketoglutarate, which is catalyzed by a homocitrate synthase encoded by nifV. By deleting the nifV gene from Azotobacter vinelandii we were able to study the role of homocitrate in nitrogenase catalysis. A poly-histidine tail was incorporated into the C-termini of the a-subunit permitting isolation of the homocitrateless MoFe protein by using metal affinity chromatography. We have found that the addition of a poly-histidine tag does not alter the catalytic behavior of the native enzyme. In NifV- strains of Klebsiella pneumoniae, citrate has been found to replace homocitrate as the organic constituent of FeMo-co. We have found no evidence this is so in A. vinelandii. Gas chromatography mass spectrophotometry studies indicate little or no organic acids are associated with FeMo-co. We examined the catalytic properties of the NifV- MoFe protein In the mutant, H2 evolution is inhibited by the addition of CO, unlike in the wild type. We have found that the NifV- MoFe protein from A. vinelandii is able to catalyze the reduction of acetylene to both ethylene and ethane.

Degree

thesis:*
Name thesis:degree_name
Master of Science
Level thesis:degree_level
masters
Discipline thesis:degree_discipline
Biochemistry and Anaerobic Microbiology
Department dc:contributor.department
Biochemistry and Anaerobic Microbiology
Grantor dc:publisher
Virginia Tech
Year dc:date.issued
1998

Author and committee

dc:creator, dc:contributor.*
Author dc:creator
  • Comaratta, Leonard M.
Chair dc:contributor.committeechair
  • Dean, Dennis R.
Committee members dc:contributor.committeemember
  • Larson, Timothy J.
  • Gregory, Eugene M.
  • Chen, Jiann-Shin
  • Claus, George William

Subjects

dc:subject × 3

Rights

dc:rights
Statement dc:rights
  • In Copyright

Identifiers

dc:identifier.*
Dc Identifier Other
etd-121598-113534
OAI identifier oai:identifier
oai:vtechworks.lib.vt.edu:10919/36177

Chain of custody

source
Harvested from
Virginia Tech
Base URL
vtechworks.lib.vt.edu/oai/request
Last updated
2026-07-22
Source record
OAI-PMH GetRecord
citation

Comaratta, Leonard M.. Characterization of an altered MoFe protein from a nifV- strain from Azotobacter vinelandii. masters thesis, Virginia Tech, 1998. http://hdl.handle.net/10919/36177