The mechanism of ADP phosphorylation by ATP synthase

• Autorzy: Weber J
• Języki publikacji: EN

Słowa kluczowe

EN

oxidative phosphorylation; phosphorylation; enzyme; phosphate; synthesis; bacteria; synthase; proton translocation; hydrolysis

• Wydawca: -
• Czasopismo: Cellular and Molecular Biology Letters
• Rocznik: 2003
• Tom: 08
• Numer: 2A
• Opis fizyczny: p.623

Twórcy

autor

Weber J

• Texas Tech University Health Sciences Center, TX 79430, USA

Bibliografia

• 1. Senior, A.E., Nadanaciva, S. and Weber, J. The molecular mechanism of ATP synthesis by F1F0-ATP synthase. Biochim. Biophys. Acta 1553 (2002) 188-211.
• 2. Weber, J., Wilke-Mounts, S., Lee, R.S.F., Grell, E. and Senior, A.E. Specific placement of tryptophan in the catalytic sites of Escherichia coli F1-ATPase provides a direct probe of nucleotide binding: Maximal ATP hydrolysis occurs with three sites occupied. J. Biol. Chem. 268 (1993) 20126-20133.
• 3. Weber, J., Hammond, S.T., Wilke-Mounts, S. and Senior, A.E. Mg2+ coordination in catalytic sites of F1-ATPase. Biochemistry 37 (1998) 608-614,
• 4. Nadanaciva, S., Weber, J., Wilke-Mounts, S. and Senior, A.E. Importance of F1-ATPase residue α-Arg-376 for catalytic transition state stabilization. Biochemistry 38 (1999) 15493-15499.