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Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria
The crystal structure of bovine mitochondrial F1-ATPase determined at 2.8 Å resolution supports a catalytic mechanism in intact ATP synthase in which the three catalytic subunits are in different states of the catalytic cycle at any instant.
Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria
- Ian N. Watt, M. G. Montgomery, M. Runswick, A. Leslie, J. Walker
- Biology, ChemistryProceedings of the National Academy of Sciences
- 16 September 2010
In fungi, eubacteria, and plant chloroplasts, ring sizes of c10–c15 subunits have been observed, implying that these enzymes need 3.3–5 protons to make each ATP, but until now no higher eukaryote has been examined.
The nuclear encoded subunits of complex I from bovine heart mitochondria.
The ATP synthase: the understood, the uncertain and the unknown.
- J. Walker
- BiologyBiochemical Society transactions
- 1 February 2013
Evidence is growing for other roles of ATP synthases in the inner membranes of mitochondria, where they form supermolecular complexes, possibly with specific lipids, and these complexes probably contribute to, or even determine, the formation of the cristae.
Structure of Bovine Mitochondrial F1-ATPase with Nucleotide Bound to All Three Catalytic Sites Implications for the Mechanism of Rotary Catalysis
Bovine Complex I Is a Complex of 45 Different Subunits*
- J. Carroll, I. Fearnley, J. Skehel, R. J. Shannon, J. Hirst, J. Walker
- Chemistry, BiologyJournal of Biological Chemistry
- 27 October 2006
The subunit composition of bovine complex I is established, a complex of 45 different proteins plus non-covalently bound FMN and eight iron-sulfur clusters and shown to be a C-terminal fragment of subunit SGDH arising from a specific peptide bond cleavage between Ile-55 and Pro-56 during the electrospray ionization process.
Structure of the Rotor of the V-Type Na+-ATPase from Enterococcus hirae
The membrane rotor ring from the vacuolar-type (V-type) sodium ion–pumping adenosine triphosphatase (Na+-ATPase) from Enterococcus hirae consists of 10 NtpK subunits, which are homologs of the…
Mechanism of inhibition of bovine F1-ATPase by resveratrol and related polyphenols
- J. Gledhill, M. G. Montgomery, A. Leslie, J. Walker
- Chemistry, BiologyProceedings of the National Academy of Sciences
- 21 August 2007
The structures of F1-ATPase from bovine heart mitochondria inhibited with the dietary phytopolyphenol, resveratrol, and with the related polyphenols quercetin and piceatannol have been determined at…
Analysis of the Subunit Composition of Complex I from Bovine Heart Mitochondria*S
- J. Carroll, I. Fearnley, R. J. Shannon, J. Hirst, J. Walker
- BiologyMolecular & Cellular Proteomics
- 1 February 2003
The presence of the known 35 nuclear encoded subunits in complex I has been confirmed, and four additional nuclear encodedSubunits have been detected, unlikely that any more subunits of the bovine complex remain undiscovered.
Mitochondrial quality control mediated by PINK1 and Parkin: links to parkinsonism.
- Derek P. Narendra, J. Walker, R. Youle
- BiologyCold Spring Harbor perspectives in biology
- 1 November 2012
The recent rapid progress in understanding the molecular mechanisms of PINK1- and Parkin-mediated mitophagy and the identification of Parkin substrates suggesting how mitochondrial fission and trafficking are involved are reviewed.