Calhoun MW - Search Results

1

Strong-field and integral spin-ligand complexes of the cytochrome bo quinol oxidase in Escherichia coli membrane preparations.

Calhoun MW, Gennis RB, Ingledew WJ, Salerno JC. Calhoun MW, et al. Biochim Biophys Acta. 1994 May 18;1206(1):143-54. doi: 10.1016/0167-4838(94)90083-3. Biochim Biophys Acta. 1994. PMID: 8186244

2

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. Biochemistry. 1992 Nov 24;31(46):11435-40. doi: 10.1021/bi00161a023. Biochemistry. 1992. PMID: 1332759

3

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: calhoun mw. J Biol Chem. 1992 Jan 25;267(3):2105-13. J Biol Chem. 1992. PMID: 1309809 Free article.

4

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. FEBS Lett. 1992 Sep 7;309(2):127-9. doi: 10.1016/0014-5793(92)81079-2. FEBS Lett. 1992. PMID: 1324191 Free article.

5

The highly conserved methionine of subunit I of the heme-copper oxidases is not at the heme-copper dinuclear center: mutagenesis of M110 in subunit I of cytochrome bo3-type ubiquinol oxidase from Escherichia coli.

Calhoun MW, Lemieux LJ, Garcia-Horsman JA, Thomas JW, Alben JO, Gennis RB. Calhoun MW, et al. FEBS Lett. 1995 Jul 24;368(3):523-5. doi: 10.1016/0014-5793(95)00696-7. FEBS Lett. 1995. PMID: 7635213 Free article.

6

The cytochrome oxidase superfamily of redox-driven proton pumps.

Calhoun MW, Thomas JW, Gennis RB. Calhoun MW, et al. Trends Biochem Sci. 1994 Aug;19(8):325-30. doi: 10.1016/0968-0004(94)90071-x. Trends Biochem Sci. 1994. PMID: 7940677 Review.

7

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: calhoun mw. Biochemistry. 1994 Nov 8;33(44):13013-21. doi: 10.1021/bi00248a010. Biochemistry. 1994. PMID: 7947706

8

Site-directed mutants of the cytochrome bo ubiquinol oxidase of Escherichia coli: amino acid substitutions for two histidines that are putative CuB ligands.

Calhoun MW, Hill JJ, Lemieux LJ, Ingledew WJ, Alben JO, Gennis RB. Calhoun MW, et al. Biochemistry. 1993 Nov 2;32(43):11524-9. doi: 10.1021/bi00094a008. Biochemistry. 1993. PMID: 8218219

9

Spectroscopic characterization of mutants supports the assignment of histidine-419 as the axial ligand of heme o in the binuclear center of the cytochrome bo ubiquinol oxidase from Escherichia coli.

Calhoun MW, Lemieux LJ, Thomas JW, Hill JJ, Goswitz VC, Alben JO, Gennis RB. Calhoun MW, et al. Biochemistry. 1993 Dec 7;32(48):13254-61. doi: 10.1021/bi00211a038. Biochemistry. 1993. PMID: 8241181

10

Identity of the axial ligand of the high-spin heme in cytochrome oxidase: spectroscopic characterization of mutants in the bo-type oxidase of Escherichia coli and the aa3-type oxidase of Rhodobacter sphaeroides.

Calhoun MW, Thomas JW, Hill JJ, Hosler JP, Shapleigh JP, Tecklenburg MM, Ferguson-Miller S, Babcock GT, Alben JO, Gennis RB. Calhoun MW, et al. Biochemistry. 1993 Oct 12;32(40):10905-11. doi: 10.1021/bi00091a046. Biochemistry. 1993. PMID: 8399240

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