Paddock ML - Search Results

1

Identification of a novel protonation pattern for carboxylic acids upon Q(B) photoreduction in Rhodobacter sphaeroides reaction center mutants at Asp-L213 and Glu-L212 sites.

Nabedryk E, Breton J, Okamura MY, Paddock ML. Nabedryk E, et al. Among authors: paddock ml. Biochemistry. 2004 Jun 15;43(23):7236-43. doi: 10.1021/bi049342y. Biochemistry. 2004. PMID: 15182169

2

Rapid-scan Fourier transform infrared spectroscopy shows coupling of GLu-L212 protonation and electron transfer to Q(B) in Rhodobacter sphaeroides reaction centers.

Mezzetti A, Nabedryk E, Breton J, Okamura MY, Paddock ML, Giacometti G, Leibl W. Mezzetti A, et al. Among authors: paddock ml. Biochim Biophys Acta. 2002 Feb 15;1553(3):320-30. doi: 10.1016/s0005-2728(02)00186-x. Biochim Biophys Acta. 2002. PMID: 11997141 Free article.

3

Interactions between cytochrome c2 and photosynthetic reaction center from Rhodobacter sphaeroides: changes in binding affinity and electron transfer rate due to mutation of interfacial hydrophobic residues are strongly correlated.

Gong XM, Paddock ML, Okamura MY. Gong XM, et al. Among authors: paddock ml. Biochemistry. 2003 Dec 16;42(49):14492-500. doi: 10.1021/bi035603c. Biochemistry. 2003. PMID: 14661961

4

An isotope-edited FTIR investigation of the role of Ser-L223 in binding quinone (QB) and semiquinone (QB-) in the reaction center from Rhodobacter sphaeroides.

Nabedryk E, Paddock ML, Okamura MY, Breton J. Nabedryk E, et al. Among authors: paddock ml. Biochemistry. 2005 Nov 8;44(44):14519-27. doi: 10.1021/bi051328d. Biochemistry. 2005. PMID: 16262252

5

Monitoring the pH dependence of IR carboxylic acid signals upon Q(B)- formation in the Glu-L212 --> Asp/Asp-L213 --> Glu swap mutant reaction center from Rhodobacter sphaeroides.

Nabedryk E, Paddock ML, Okamura MY, Breton J. Nabedryk E, et al. Among authors: paddock ml. Biochemistry. 2007 Feb 6;46(5):1176-82. doi: 10.1021/bi0619627. Biochemistry. 2007. PMID: 17260947

6

Interaction between cytochrome c2 and the photosynthetic reaction center from Rhodobacter sphaeroides: role of interprotein hydrogen bonds in binding and electron transfer.

Abresch EC, Paddock ML, Villalobos M, Chang C, Okamura MY. Abresch EC, et al. Among authors: paddock ml. Biochemistry. 2008 Dec 16;47(50):13318-25. doi: 10.1021/bi801675a. Biochemistry. 2008. PMID: 19053264 Free PMC article.

7

Identification of FTIR bands due to internal water molecules around the quinone binding sites in the reaction center from Rhodobacter sphaeroides.

Iwata T, Paddock ML, Okamura MY, Kandori H. Iwata T, et al. Among authors: paddock ml. Biochemistry. 2009 Feb 17;48(6):1220-9. doi: 10.1021/bi801990s. Biochemistry. 2009. PMID: 19161296 Free PMC article.

8

Effect of metal binding on electrogenic proton transfer associated with reduction of the secondary electron acceptor (QB) in Rhodobacter sphaeroides chromatophores.

Keller S, Beatty JT, Paddock M, Breton J, Leibl W. Keller S, et al. Biochemistry. 2001 Jan 16;40(2):429-39. doi: 10.1021/bi001286n. Biochemistry. 2001. PMID: 11148037

9

Pathway of proton transfer in bacterial reaction centers: further investigations on the role of Ser-L223 studied by site-directed mutagenesis.

Paddock ML, Feher G, Okamura MY. Paddock ML, et al. Biochemistry. 1995 Dec 5;34(48):15742-50. doi: 10.1021/bi00048a019. Biochemistry. 1995. PMID: 7495805

10

Fourier transforms infrared difference spectroscopy of secondary quinone acceptor photoreduction in proton transfer mutants of Rhodobacter sphaeroides.

Nabedryk E, Breton J, Hienerwadel R, Fogel C, Mäntele W, Paddock ML, Okamura MY. Nabedryk E, et al. Among authors: paddock ml. Biochemistry. 1995 Nov 14;34(45):14722-32. doi: 10.1021/bi00045a013. Biochemistry. 1995. PMID: 7578080

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