Smulevich G - Search Results

1

Alteration of the proximal bond energy in the unliganded form of the homodimeric myoglobin from Nassa mutabilis. Kinetic and spectroscopic evidence.

Coletta M, Ascenzi P, Smulevich G, Mantini AR, Del Gaudio R, Piscopo M, Geraci G. Coletta M, et al. Among authors: smulevich g. FEBS Lett. 1992 Jan 20;296(2):184-6. doi: 10.1016/0014-5793(92)80375-q. FEBS Lett. 1992. PMID: 1733775 Free article.

2

Iron insertion into coproporphyrin III-ferrochelatase complex: Evidence for an intermediate distorted catalytic species.

Gabler T, Dali A, Sebastiani F, Furtmüller PG, Becucci M, Hofbauer S, Smulevich G. Gabler T, et al. Among authors: smulevich g. Protein Sci. 2023 Nov;32(11):e4788. doi: 10.1002/pro.4788. Protein Sci. 2023. PMID: 37743577 Free PMC article.

3

Resonance Raman investigation of ferric iron in horseradish peroxidase and its aromatic donor complexes at room and low temperatures.

Smulevich G, English AM, Mantini AR, Marzocchi MP. Smulevich G, et al. Biochemistry. 1991 Jan 22;30(3):772-9. doi: 10.1021/bi00217a029. Biochemistry. 1991. PMID: 1988064

4

CO dissociation in cytochrome c peroxidase: site-directed mutagenesis shows that distal Arg 48 influences CO dissociation rates.

Miller MA, Mauro JM, Smulevich G, Coletta M, Kraut J, Traylor TG. Miller MA, et al. Among authors: smulevich g. Biochemistry. 1990 Oct 23;29(42):9978-88. doi: 10.1021/bi00494a031. Biochemistry. 1990. PMID: 2176859

5

Effects of temperature and glycerol on the resonance Raman spectra of cytochrome c peroxidase and selected mutants.

Smulevich G, Mantini AR, English AM, Mauro JM. Smulevich G, et al. Biochemistry. 1989 Jun 13;28(12):5058-64. doi: 10.1021/bi00438a024. Biochemistry. 1989. PMID: 2548600

6

Resonance Raman studies of the heme active site of the homodimeric myoglobin from Nassa mutabilis: a peculiar case.

Smulevich G, Mantini AR, Paoli M, Coletta M, Geraci G. Smulevich G, et al. Biochemistry. 1995 Jun 6;34(22):7507-16. doi: 10.1021/bi00022a026. Biochemistry. 1995. PMID: 7779795

7

Spectroscopic evidence for a conformational transition in horseradish peroxidase at very low pH.

Smulevich G, Paoli M, De Sanctis G, Mantini AR, Ascoli F, Coletta M. Smulevich G, et al. Biochemistry. 1997 Jan 21;36(3):640-9. doi: 10.1021/bi960427b. Biochemistry. 1997. PMID: 9012679

8

pH dependence of structural and functional properties of oxidized cytochrome c" from Methylophilus methylotrophus.

Coletta M, Costa H, De Sanctis G, Neri F, Smulevich G, Turner DL, Santos H. Coletta M, et al. Among authors: smulevich g. J Biol Chem. 1997 Oct 3;272(40):24800-4. doi: 10.1074/jbc.272.40.24800. J Biol Chem. 1997. PMID: 9312076 Free article.

9

Cooperative mechanism in the homodimeric myoglobin from Nassa mutabilis.

Coletta M, Ascenzi P, Polizio F, Smulevich G, del Gaudio R, Piscopo M, Geraci G. Coletta M, et al. Among authors: smulevich g. Biochemistry. 1998 Mar 3;37(9):2873-8. doi: 10.1021/bi9713613. Biochemistry. 1998. PMID: 9485438

10

Anion- and pH-linked conformational transition in horseradish peroxidase.

Priori AM, Indiani C, De Sanctis G, Marini S, Santucci R, Smulevich G, Coletta M. Priori AM, et al. Among authors: smulevich g. J Inorg Biochem. 2000 Apr;79(1-4):25-30. doi: 10.1016/s0162-0134(99)00229-9. J Inorg Biochem. 2000. PMID: 10830843

In a previous study we have shown that bringing horseradish peroxidase to pH 3.0 induces a spectroscopic transition (G. Smulevich et al., Biochemistry 36 (1997) 640). We have extended the investigation on this pH-linked conformational change to different experimenta …

In a previous study we have shown that bringing horseradish peroxidase to pH 3.0 induces a spectroscopic transition (G. Smulevich …

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