Structural biology. PMF through the redox loop.
Richardson
David
D
School of Biological Sciences, University of East Anglia, Norwich Research Park, Norwich NR4 7TJ, UK. d.richardson@uea.ac.uk
Sawers
Gary
G
D001665:Binding Sites; D002384:Catalysis; D020134:Catalytic Domain; D002462:Cell Membrane / Q000201:enzymology; D018360:Crystallography, X-Ray; D004579:Electron Transport; D004926:Escherichia coli / Q000201:enzymology* / Q000378:metabolism; D005560:Formate Dehydrogenases / Q000737:chemistry* / Q000378:metabolism; D005561:Formates / Q000378:metabolism; D006150:Guanine Nucleotides / Q000378:metabolism; D006860:Hydrogen Bonding; D007506:Iron-Sulfur Proteins / Q000737:chemistry / Q000378:metabolism; D008564:Membrane Potentials; D009566:Nitrates / Q000378:metabolism; D009942:Organometallic Compounds / Q000378:metabolism; D010084:Oxidation-Reduction; D011487:Protein Conformation; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D018892:Proton-Motive Force; D011522:Protons; D024482:Vitamin K 2 / Q000378:metabolism
D005561:Formates; D006150:Guanine Nucleotides; D007506:Iron-Sulfur Proteins; D009566:Nitrates; D009942:Organometallic Compounds; D011522:Protons; C106961:bis(molybdopterin guanine dinucleotide)molybdenum; C030544:formic acid; D024482:Vitamin K 2; D005560:Formate Dehydrogenases