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Differential nucleotide binding to catalytic and noncatalytic sites and related conformational changes involving alpha/beta-subunit interactions as monitored by sensitive intrinsic fluorescence in Schizosaccharomyces pombe mitochondrial F1.
Divita G, Di Pietro A, Roux B, Gautheron DC. Divita G, et al. Among authors: di pietro a. Biochemistry. 1992 Jun 30;31(25):5791-8. doi: 10.1021/bi00140a015. Biochemistry. 1992. PMID: 1319203
Mitochondrial F1 from the yeast Schizosaccharomyces pombe exhibits an intrinsic tryptophan fluorescence sensitive to adenine nucleotides and inorganic phosphate [Divita, G., Di Pietro, A., Deleage, G., Roux, B., & Gautheron, D.C. (1991) Biochemistry 30, 3 …
Mitochondrial F1 from the yeast Schizosaccharomyces pombe exhibits an intrinsic tryptophan fluorescence sensitive to adenine nucleotides and …
Fate of nucleotides bound to reconstituted Fo-F1 during adenosine 5'-triphosphate synthesis activation or hydrolysis: role of protein inhibitor and hysteretic inhibition.
Penin F, Di Pietro A, Godinot C, Gautheron DC. Penin F, et al. Among authors: di pietro a. Biochemistry. 1988 Dec 13;27(25):8969-74. doi: 10.1021/bi00425a014. Biochemistry. 1988. PMID: 2906804
The protein ATPase inhibitor entraps about five nucleotides in pig heart mitochondrial F1, one at least being a triphosphate [Di Pietro, A., Penin, F., Julliard, J.H., Godinot, C., & Gautheron, D.C. (1988) Biochem. ...In contrast, under ATP synthes …
The protein ATPase inhibitor entraps about five nucleotides in pig heart mitochondrial F1, one at least being a triphosphate [Di
523 results