Asso M - Search Results

1

Study of the spin-spin interactions between the metal centers of Desulfovibrio gigas aldehyde oxidoreductase: identification of the reducible sites of the [2Fe-2S]1+,2+ clusters.

More C, Asso M, Roger G, Guigliarelli B, Caldeira J, Moura J, Bertrand P. More C, et al. Among authors: asso m. Biochemistry. 2005 Aug 30;44(34):11628-35. doi: 10.1021/bi0510025. Biochemistry. 2005. PMID: 16114900

2

EPR and redox characterization of iron-sulfur centers in nitrate reductases A and Z from Escherichia coli. Evidence for a high-potential and a low-potential class and their relevance in the electron-transfer mechanism.

Guigliarelli B, Asso M, More C, Augier V, Blasco F, Pommier J, Giordano G, Bertrand P. Guigliarelli B, et al. Among authors: asso m. Eur J Biochem. 1992 Jul 1;207(1):61-8. doi: 10.1111/j.1432-1033.1992.tb17020.x. Eur J Biochem. 1992. PMID: 1321049 Free article.

3

EPR study of the redox interactions in cytochrome c3 from Desulfovibrio vulgaris Miyazaki.

Benosman H, Asso M, Bertrand P, Yagi T, Gayda JP. Benosman H, et al. Among authors: asso m. Eur J Biochem. 1989 Jun 1;182(1):51-5. doi: 10.1111/j.1432-1033.1989.tb14799.x. Eur J Biochem. 1989. PMID: 2543574 Free article.

4

EPR determination of interaction redox potentials in a multiheme cytochrome: cytochrome c3 from Desulfovibrio desulfuricans Norway.

Gayda JP, Benosman H, Bertrand P, More C, Asso M. Gayda JP, et al. Among authors: asso m. Eur J Biochem. 1988 Oct 15;177(1):199-206. doi: 10.1111/j.1432-1033.1988.tb14362.x. Eur J Biochem. 1988. PMID: 2846296 Free article.

5

Structural organization of the Ni and (4Fe-4S) centers in the active form of Desulfovibrio gigas hydrogenase. Analysis of the magnetic interactions by electron paramagnetic resonance spectroscopy.

Guigliarelli B, More C, Fournel A, Asso M, Hatchikian EC, Williams R, Cammack R, Bertrand P. Guigliarelli B, et al. Among authors: asso m. Biochemistry. 1995 Apr 11;34(14):4781-90. doi: 10.1021/bi00014a036. Biochemistry. 1995. PMID: 7718585

6

Site-directed mutagenesis of conserved cysteine residues within the beta subunit of Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of the mutated enzymes.

Augier V, Guigliarelli B, Asso M, Bertrand P, Frixon C, Giordano G, Chippaux M, Blasco F. Augier V, et al. Among authors: asso m. Biochemistry. 1993 Mar 2;32(8):2013-23. doi: 10.1021/bi00059a018. Biochemistry. 1993. PMID: 8383531

7

Removal of the high-potential [4Fe-4S] center of the beta-subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutated enzymes.

Augier V, Asso M, Guigliarelli B, More C, Bertrand P, Santini CL, Blasco F, Chippaux M, Giordano G. Augier V, et al. Among authors: asso m. Biochemistry. 1993 May 18;32(19):5099-108. doi: 10.1021/bi00070a018. Biochemistry. 1993. PMID: 8388253

8

Complete coordination of the four Fe-S centers of the beta subunit from Escherichia coli nitrate reductase. Physiological, biochemical, and EPR characterization of site-directed mutants lacking the highest or lowest potential [4Fe-4S] clusters.

Guigliarelli B, Magalon A, Asso M, Bertrand P, Frixon C, Giordano G, Blasco F. Guigliarelli B, et al. Among authors: asso m. Biochemistry. 1996 Apr 16;35(15):4828-36. doi: 10.1021/bi952459p. Biochemistry. 1996. PMID: 8664273

9

Molybdenum cofactor properties and [Fe-S] cluster coordination in Escherichia coli nitrate reductase A: investigation by site-directed mutagenesis of the conserved his-50 residue in the NarG subunit.

Magalon A, Asso M, Guigliarelli B, Rothery RA, Bertrand P, Giordano G, Blasco F. Magalon A, et al. Among authors: asso m. Biochemistry. 1998 May 19;37(20):7363-70. doi: 10.1021/bi972858f. Biochemistry. 1998. PMID: 9585550

10

Analysis of the electron paramagnetic resonance properties of the [2Fe-2S]1+ centers in molybdenum enzymes of the xanthine oxidase family: assignment of signals I and II.

Caldeira J, Belle V, Asso M, Guigliarelli B, Moura I, Moura JJ, Bertrand P. Caldeira J, et al. Among authors: asso m. Biochemistry. 2000 Mar 14;39(10):2700-7. doi: 10.1021/bi9921485. Biochemistry. 2000. PMID: 10704221

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