Probing a hydrogen bond pair and the FAD redox properties in the proline dehydrogenase domain of Escherichia coli PutA.
Baban
Berevan A
BA
Department of Chemistry and Biochemistry, University of Missouri-St. Louis, St. Louis, MO 63121, USA.
Vinod
Madhavan P
MP
Tanner
John J
JJ
Becker
Donald F
DF
D001426:Bacterial Proteins / Q000378:metabolism*; D001665:Binding Sites; D004563:Electrochemistry; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics / Q000378:metabolism; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism*; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008565:Membrane Proteins / Q000378:metabolism*; D010084:Oxidation-Reduction; D011394:Proline Oxidase / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D013057:Spectrum Analysis
D001426:Bacterial Proteins; D008565:Membrane Proteins; C080683:PutA protein, Bacteria; D005182:Flavin-Adenine Dinucleotide; D011394:Proline Oxidase