Gennis RB - Search Results

1

Site-directed mutagenesis of residues within helix VI in subunit I of the cytochrome bo3 ubiquinol oxidase from Escherichia coli suggests that tyrosine 288 may be a CuB ligand.

Thomas JW, Calhoun MW, Lemieux LJ, Puustinen A, Wikström M, Alben JO, Gennis RB. Thomas JW, et al. Among authors: gennis rb. Biochemistry. 1994 Nov 8;33(44):13013-21. doi: 10.1021/bi00248a010. Biochemistry. 1994. PMID: 7947706

2

Determination of the ligands of the low spin heme of the cytochrome o ubiquinol oxidase complex using site-directed mutagenesis.

Lemieux LJ, Calhoun MW, Thomas JW, Ingledew WJ, Gennis RB. Lemieux LJ, et al. Among authors: gennis rb. J Biol Chem. 1992 Jan 25;267(3):2105-13. J Biol Chem. 1992. PMID: 1309809 Free article.

3

Spectroscopic and genetic evidence for two heme-Cu-containing oxidases in Rhodobacter sphaeroides.

Shapleigh JP, Hill JJ, Alben JO, Gennis RB. Shapleigh JP, et al. Among authors: gennis rb. J Bacteriol. 1992 Apr;174(7):2338-43. doi: 10.1128/jb.174.7.2338-2343.1992. J Bacteriol. 1992. PMID: 1313003 Free PMC article.

4

Cloning, sequencing and deletion from the chromosome of the gene encoding subunit I of the aa3-type cytochrome c oxidase of Rhodobacter sphaeroides.

Shapleigh JP, Gennis RB. Shapleigh JP, et al. Among authors: gennis rb. Mol Microbiol. 1992 Mar;6(5):635-42. doi: 10.1111/j.1365-2958.1992.tb01511.x. Mol Microbiol. 1992. PMID: 1313140

5

Examination of the functional roles of 5 highly conserved residues in the cytochrome b subunit of the bc1 complex of Rhodobacter sphaeroides.

Yun CH, Wang Z, Crofts AR, Gennis RB. Yun CH, et al. Among authors: gennis rb. J Biol Chem. 1992 Mar 25;267(9):5901-9. J Biol Chem. 1992. PMID: 1313421 Free article.

6

Definition of the catalytic site of cytochrome c oxidase: specific ligands of heme a and the heme a3-CuB center.

Shapleigh JP, Hosler JP, Tecklenburg MM, Kim Y, Babcock GT, Gennis RB, Ferguson-Miller S. Shapleigh JP, et al. Among authors: gennis rb. Proc Natl Acad Sci U S A. 1992 Jun 1;89(11):4786-90. doi: 10.1073/pnas.89.11.4786. Proc Natl Acad Sci U S A. 1992. PMID: 1317571 Free PMC article.

7

Modified, large-scale purification of the cytochrome o complex (bo-type oxidase) of Escherichia coli yields a two heme/one copper terminal oxidase with high specific activity.

Minghetti KC, Goswitz VC, Gabriel NE, Hill JJ, Barassi CA, Georgiou CD, Chan SI, Gennis RB. Minghetti KC, et al. Among authors: gennis rb. Biochemistry. 1992 Aug 4;31(30):6917-24. doi: 10.1021/bi00145a008. Biochemistry. 1992. PMID: 1322173

8

Restoration of a lost metal-binding site: construction of two different copper sites into a subunit of the E. coli cytochrome o quinol oxidase complex.

van der Oost J, Lappalainen P, Musacchio A, Warne A, Lemieux L, Rumbley J, Gennis RB, Aasa R, Pascher T, Malmström BG, et al. van der Oost J, et al. Among authors: gennis rb. EMBO J. 1992 Sep;11(9):3209-17. doi: 10.1002/j.1460-2075.1992.tb05398.x. EMBO J. 1992. PMID: 1324168 Free PMC article.

9

The formate complex of the cytochrome bo quinol oxidase of Escherichia coli exhibits a 'g = 12' EPR feature analogous to that of 'slow' cytochrome oxidase.

Calhoun MW, Gennis RB, Salerno JC. Calhoun MW, et al. Among authors: gennis rb. FEBS Lett. 1992 Sep 7;309(2):127-9. doi: 10.1016/0014-5793(92)81079-2. FEBS Lett. 1992. PMID: 1324191 Free article.

10

Demonstration by FTIR that the bo-type ubiquinol oxidase of Escherichia coli contains a heme-copper binuclear center similar to that in cytochrome c oxidase and that proper assembly of the binuclear center requires the cyoE gene product.

Hill J, Goswitz VC, Calhoun M, Garcia-Horsman JA, Lemieux L, Alben JO, Gennis RB. Hill J, et al. Among authors: gennis rb. Biochemistry. 1992 Nov 24;31(46):11435-40. doi: 10.1021/bi00161a023. Biochemistry. 1992. PMID: 1332759

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