Affiliation: University of Illinois
- Expression and mutagenesis of the NqrC subunit of the NQR respiratory Na(+) pump from Vibrio cholerae with covalently attached FMNB Barquera
Department of Biochemistry, University of Illinois at Urbana Champaign, Urbana, 61801, USA
FEBS Lett 492:45-9. 2001..In contrast, no covalent flavin was detected when threonine-225 was replaced by leucine. The data show that the FMN attachment does not require assembly of the enzyme and are consistent with the unusual threonine attachment site...
- Direct evidence for the protonation of aspartate-75, proposed to be at a quinol binding site, upon reduction of cytochrome bo3 from Escherichia coliP Hellwig
Department of Biochemistry, University of Illinois, 600 South Mathews Avenue, Urbana, Illinois 61801 3364, USA
Biochemistry 40:1077-82. 2001..It is suggested that upon reduction of the bound ubiquinone at the high affinity site, D75 takes up a proton, possibly sharing it with ubiquinol...
- Pathways for proton release during ubihydroquinone oxidation by the bc(1) complexA R Crofts
Department of Biochemistry, University of Illinois at Urbana Champaign, Urbana, IL 61801, USA
Proc Natl Acad Sci U S A 96:10021-6. 1999..H(+) transfer from semiquinone to the carboxylate side chain and rotation to the position found in the myxothiazol structure provide a pathway for release of the second proton...
- Glutamate-89 in subunit II of cytochrome bo3 from Escherichia coli is required for the function of the heme-copper oxidaseJ Ma
Department of Biochemistry, University of Illinois, Urbana 61801, USA
Biochemistry 38:15150-6. 1999..Thus, it appears that the inhibition resulting from the E89II mutation is due to a block in the reduction of the heme-copper binuclear center, expected for K-channel mutants...
- The cbb3-type cytochrome c oxidase from Rhodobacter sphaeroides, a proton-pumping heme-copper oxidaseM Toledo-Cuevas
Departamento de Bioquimica, UNAM, Ciudad Universitaria, Mexico D F, Mexico
Biochim Biophys Acta 1365:421-34. 1998..Analysis of proton translocation in several strains shows that cytochrome cbb3 is a proton pump. We also conclude that cytochromes cbb3 and aa3 are the only cytochrome c oxidases in the respiratory chain of R. sphaeroides...
- The Na+ and K+ transport deficiency of an E. coli mutant lacking the NhaA and NhaB proteins is apparent and caused by impaired osmoregulationM L Verkhovskaya
Department of Medical Chemistry, Institute of Biomedical Sciences, University of Helsinki, Finland
FEBS Lett 439:271-4. 1998..We suggest that this mutant is primarily deficient in osmoregulation rather than in cation transport per se...
- Sodium-dependent steps in the redox reactions of the Na+-motive NADH:quinone oxidoreductase from Vibrio harveyiA V Bogachev
Department of Bioenergetics, A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, Russia
Biochemistry 40:7318-23. 2001..These data led us to conclude that the sodium-dependent step within the Na+-NQR is located between the noncovalently bound FAD and the covalently bound FMN...