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Catalytic sector of complex I (NADH:ubiquinone oxidoreductase): subunit stoichiometry and substrate-induced conformation changes.

Belogrudov G, Hatefi Y. Belogrudov G, et al. Biochemistry. 1994 Apr 19;33(15):4571-6. doi: 10.1021/bi00181a018. Biochemistry. 1994. PMID: 8161512

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Factor B and the mitochondrial ATP synthase complex.

Belogrudov GI, Hatefi Y. Belogrudov GI, et al. J Biol Chem. 2002 Feb 22;277(8):6097-103. doi: 10.1074/jbc.M111256200. Epub 2001 Dec 14. J Biol Chem. 2002. PMID: 11744738 Free article.

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Factor B is essential for ATP synthesis by mitochondria.

Belogrudov GI. Belogrudov GI. Arch Biochem Biophys. 2002 Oct 15;406(2):271-4. doi: 10.1016/s0003-9861(02)00431-9. Arch Biochem Biophys. 2002. PMID: 12361715

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The multiple nicotinamide nucleotide-binding subunits of bovine heart mitochondrial NADH:ubiquinone oxidoreductase (complex I).

Yamaguchi M, Belogrudov GI, Matsuno-Yagi A, Hatefi Y. Yamaguchi M, et al. Among authors: belogrudov gi. Eur J Biochem. 2000 Jan;267(2):329-36. doi: 10.1046/j.1432-1327.2000.00999.x. Eur J Biochem. 2000. PMID: 10632702

Our previous studies had shown that this subunit also binds NADP, but not NAD(H) [Yamaguchi, M., Belogrudov, G.I. & Hatefi, Y. (1998) J. Biol. Chem. 273, 8094-8098]. ...

Our previous studies had shown that this subunit also binds NADP, but not NAD(H) [Yamaguchi, M., Belogrudov, G.I. & Hatefi …

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Mitochondrial NADH-ubiquinone oxidoreductase (Complex I). Effect of substrates on the fragmentation of subunits by trypsin.

Yamaguchi M, Belogrudov GI, Hatefi Y. Yamaguchi M, et al. Among authors: belogrudov gi. J Biol Chem. 1998 Apr 3;273(14):8094-8. doi: 10.1074/jbc.273.14.8094. J Biol Chem. 1998. PMID: 9525911

Results shown elsewhere on changes in the cross-linking pattern of complex I subunits when the enzyme was pretreated with NADH or NADPH (Belogrudov, G., and Hatefi, Y. (1994) Biochemistry 33, 4571-4576) also indicated that complex I undergoes extensive conformation …

Results shown elsewhere on changes in the cross-linking pattern of complex I subunits when the enzyme was pretreated with NADH or NADPH ( …

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Intersubunit interactions in the bovine mitochondrial complex I as revealed by ligand blotting.

Belogrudov GI, Hatefi Y. Belogrudov GI, et al. Biochem Biophys Res Commun. 1996 Oct 3;227(1):135-9. doi: 10.1006/bbrc.1996.1479. Biochem Biophys Res Commun. 1996. PMID: 8858115

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Mitochondrial ATP synthase: Fe2+-catalyzed fragmentation of the soluble F1-ATPase.

Belogrudov GI. Belogrudov GI. Arch Biochem Biophys. 1996 Nov 1;335(1):131-8. doi: 10.1006/abbi.1996.0490. Arch Biochem Biophys. 1996. PMID: 8914843

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Membrane topography and near-neighbor relationships of the mitochondrial ATP synthase subunits e, f, and g.

Belogrudov GI, Tomich JM, Hatefi Y. Belogrudov GI, et al. J Biol Chem. 1996 Aug 23;271(34):20340-5. doi: 10.1074/jbc.271.34.20340. J Biol Chem. 1996. PMID: 8702768

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ATP synthase complex. Proximities of subunits in bovine submitochondrial particles.

Belogrudov GI, Tomich JM, Hatefi Y. Belogrudov GI, et al. J Biol Chem. 1995 Feb 3;270(5):2053-60. doi: 10.1074/jbc.270.5.2053. J Biol Chem. 1995. PMID: 7836433

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The proximal N-terminal amino acid residues are required for the coupling activity of the bovine heart mitochondrial factor B.

Belogrudov GI. Belogrudov GI. Arch Biochem Biophys. 2008 May 1;473(1):76-87. doi: 10.1016/j.abb.2008.02.022. Epub 2008 Feb 23. Arch Biochem Biophys. 2008. PMID: 18319055 Free PMC article.

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