Paddock ML - Search Results

1

Characterization of a highly purified, fully active, crystallizable RC-LH1-PufX core complex from Rhodobacter sphaeroides.

Abresch EC, Axelrod HL, Beatty JT, Johnson JA, Nechushtai R, Paddock ML. Abresch EC, et al. Among authors: paddock ml. Photosynth Res. 2005 Nov;86(1-2):61-70. doi: 10.1007/s11120-005-5106-z. Photosynth Res. 2005. PMID: 16172926

2

Quinone (QB) reduction by B-branch electron transfer in mutant bacterial reaction centers from Rhodobacter sphaeroides: quantum efficiency and X-ray structure.

Paddock ML, Chang C, Xu Q, Abresch EC, Axelrod HL, Feher G, Okamura MY. Paddock ML, et al. Biochemistry. 2005 May 10;44(18):6920-8. doi: 10.1021/bi047559m. Biochemistry. 2005. PMID: 15865437

3

Reaction centers from three herbicide-resistant mutants of Rhodobacter sphaeroides 2.4.1: sequence analysis and preliminary characterization.

Paddock ML, Rongey SH, Abresch EC, Feher G, Okamura MY. Paddock ML, et al. Photosynth Res. 1988 Jul;17(1-2):75-96. doi: 10.1007/BF00047682. Photosynth Res. 1988. PMID: 24429662

4

X-Ray structure determination of three mutants of the bacterial photosynthetic reaction centers from Rb. sphaeroides; altered proton transfer pathways.

Xu Q, Axelrod HL, Abresch EC, Paddock ML, Okamura MY, Feher G. Xu Q, et al. Among authors: paddock ml. Structure. 2004 Apr;12(4):703-15. doi: 10.1016/j.str.2004.03.001. Structure. 2004. PMID: 15062092 Free article.

5

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.

6

The novel 2Fe-2S outer mitochondrial protein mitoNEET displays conformational flexibility in its N-terminal cytoplasmic tethering domain.

Conlan AR, Paddock ML, Axelrod HL, Cohen AE, Abresch EC, Wiley S, Roy M, Nechushtai R, Jennings PA. Conlan AR, et al. Among authors: paddock ml. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Jul 1;65(Pt 7):654-9. doi: 10.1107/S1744309109019605. Epub 2009 Jun 27. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009. PMID: 19574633 Free PMC article.

7

Electron transfer from cytochrome c(2) to the reaction center: a transition state model for ionic strength effects due to neutral mutations.

Abresch EC, Gong XM, Paddock ML, Okamura MY. Abresch EC, et al. Among authors: paddock ml. Biochemistry. 2009 Dec 8;48(48):11390-8. doi: 10.1021/bi901332t. Biochemistry. 2009. PMID: 19877711 Free PMC article.

8

Determination of the binding sites of the proton transfer inhibitors Cd2+ and Zn2+ in bacterial reaction centers.

Axelrod HL, Abresch EC, Paddock ML, Okamura MY, Feher G. Axelrod HL, et al. Among authors: paddock ml. Proc Natl Acad Sci U S A. 2000 Feb 15;97(4):1542-7. doi: 10.1073/pnas.97.4.1542. Proc Natl Acad Sci U S A. 2000. PMID: 10677497 Free PMC article.

9

Identification of the proton pathway in bacterial reaction centers: cooperation between Asp-M17 and Asp-L210 facilitates proton transfer to the secondary quinone (QB).

Paddock ML, Adelroth P, Chang C, Abresch EC, Feher G, Okamura MY. Paddock ML, et al. Biochemistry. 2001 Jun 12;40(23):6893-902. doi: 10.1021/bi010280a. Biochemistry. 2001. PMID: 11389604

10

Identification of the proton pathway in bacterial reaction centers: decrease of proton transfer rate by mutation of surface histidines at H126 and H128 and chemical rescue by imidazole identifies the initial proton donors.

Adelroth P, Paddock ML, Tehrani A, Beatty JT, Feher G, Okamura MY. Adelroth P, et al. Among authors: paddock ml. Biochemistry. 2001 Dec 4;40(48):14538-46. doi: 10.1021/bi011585s. Biochemistry. 2001. PMID: 11724567

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