Probing mechanisms of catalysis and electron transfer by methylamine dehydrogenase by site-directed mutagenesis of αphe55

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1647, Issue 1-2, 2003, Pages 230-233

  Davidson, Victor L ^a  

^a UNIVERSITY OF MISSISSIPPI MEDICAL CENTER   (United States)

Author keywords

Copper; Enzyme; Metalloprotein; Monovalent cation; Quinone; Tryptophan

Indexed keywords

AMINE DEHYDROGENASE; PHENYLALANINE; OXIDOREDUCTASE; POTASSIUM; SODIUM;

CATALYSIS; CONFERENCE PAPER; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME LOCALIZATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ENZYME SUBUNIT; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; BINDING SITE; CHEMISTRY; METABOLISM; REVIEW; STRUCTURE ACTIVITY RELATION;

BINDING SITES; CATALYSIS; MUTAGENESIS, SITE-DIRECTED; OXIDOREDUCTASES ACTING ON CH-NH GROUP DONORS; POTASSIUM; SODIUM; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 0037974649     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1570-9639(03)00056-6     Document Type: Conference Paper

References (26)

1. Davidson V.L. Pyrroloquinoline quinone (PQQ) from methanol dehydrogenase and tryptophan tryptophylquinone (TTQ) from methylamine dehydrogenase. Adv. Protein Chem. 58:2001;95-140.
2. McIntire W.S., Wemmer D.E., Chistoserdov A., Lidstrom M.E. A new cofactor in a prokaryotic enzyme: tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase. Science. 252:1991;817-824.
3. Chen L., Doi M., Durley R.C., Chistoserdov A.Y., Lidstrom M.E., Davidson V.L., Mathews F.S. Refined crystal structure of methylamine dehydrogenase from Paracoccus denitrificans at 1.75 Å resolution. J. Mol. Biol. 276:1998;131-149.
4. Husain M., Davidson V.L. An inducible periplasmic blue copper protein from Paracoccus denitrificans. Purification, properties and physiological role. J. Biol. Chem. 260:1985;14626-14629.
5. Brooks H.B., Davidson V.L. Kinetic and thermodynamic analysis of a physiologic intermolecular electron transfer reaction between methylamine dehydrogenase and amicyanin. Biochemistry. 33:1994;5696-5701.
6. Brooks H.B., Davidson V.L. Free energy dependence of the electron transfer reaction between methylamine dehydrogenase and amicyanin. J. Am. Chem. Soc. 116:1994;11201-11202.
7. Bishop G.R., Davidson V.L. Intermolecular electron transfer from substrate-reduced methylamine dehydrogenase to amicyanin is linked to proton transfer. Biochemistry. 34:1995;12082-12086.
8. Bishop G.R., Davidson V.L. Catalytic role of monovalent cations in the mechanism of proton transfer which gates an interprotein electron transfer reaction. Biochemistry. 36:1997;13586-13592.
9. Brooks H.B., Jones L.H., Davidson V.L. Stopped-flow kinetic and deuterium kinetic isotope effect studies of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans. Biochemistry. 32:1993;2725-2729.
10. Zhu Z., Davidson V.L. Identification of a new reaction intermediate in the oxidation of methylamine dehydrogenase by amicyanin. Biochemistry. 38:1999;4862-4867.
11. Davidson V.L. Methylamine dehydrogenases from methylotrophic bacteria. Methods Enzymol. 188:1990;241-246.
12. Zhu Z., Jones L.H., Graichen M.E., Davidson V.L. Molecular basis for complex formation between methylamine dehydrogenase and amicyanin revealed by inverse mutagenesis of an interprotein salt bridge. Biochemistry. 39:2000;8830-8836.
13. Graichen M.E., Jones L.H., Sharma B.V., van Spanning R.J., Hosler J.P., Davidson V.L. Heterologous expression of correctly assembled methylamine dehydrogenase in Rhodobacter sphaeroides. J. Bacteriol. 181:1999;4216-4222.
14. Bishop G.R., Davidson V.L. Electron transfer from the aminosemiquinone reaction intermediate of methylamine dehydrogenase to amicyanin. Biochemistry. 37:1998;11026-11032.
15. 15N-NMR of the tryptophan tryptophylquinone aminoquinol reaction intermediate of methylamine dehydrogenase. J. Am. Chem. Soc. 118:1996;12868-12869.
16. Huizinga E.G., van Zanten B.A.M., Duine J.A., Jongejan J.A., Huitema F., Wilson K.S., Hol W.G.J. Active site structure of methylamine dehydrogenase; hydrazines identify C6 as the reactive site of the tryptophan-derived cofactor. Biochemistry. 31:1992;9789-9795.
17. Sun D., Jones L.H., Mathews F.S., Davidson V.L. Active site residues are critical to the folding and stability of methylamine dehydrogenase. Protein Eng. 14:2001;675-681.
18. Zhu Z., Sun D., Davidson V.L. Conversion of methylamine dehydrogenase to a long-chain amine dehydrogenase by mutagenesis of a single residue. Biochemistry. 39:2000;11184-11186.
19. Wang Y., Sun D., Davidson V.L. Use of indirect site-directed mutagenesis to alter the substrate specificity of methylamine dehydrogenase. J. Biol. Chem. 277:2002;4119-4122.
20. Kuusk V., McIntire W.S. Influence of monovalent cations on the ultraviolet-visible spectrum of tryptophan tryptophylquinone-containing methylamine dehydrogenase from bacterium W3A1. J. Biol. Chem. 269:1994;26136-26143.
21. Gorren A.C., Duine J.A. The effects of pH and cations on the spectral and kinetic properties of methylamine dehydrogenase from Thiobacillus versutus. Biochemistry. 33:1994;12202-12209.
22. Davidson V.L., Zhu Z. Reaction products and intermediates of tryptophan tryptophylquinone enzymes. J. Mol. Catal., B Enzym. 8:2000;69-83.
23. Zhu Z., Davidson V.L. Kinetic and chemical mechanisms for the effects of monovalent cations on the spectral properties of aromatic amine dehydrogenase. Biochem. J. 329:1998;175-182.
24. Sun D., Davidson V.L. Re-engineering monovalent cation binding sites of methylamine dehydrogenase: effects on spectral properties and gated electron transfer. Biochemistry. 40:2001;12285-12291.
25. Labesse G., Ferrari D., Chen Z.-W., Rossi G.L., Kuusk V., McIntire W.S., Mathews F.S. Crystallographic and spectroscopic studies of native, aminoquinol, and monovalent cation-bound forms of methylamine dehydrogenase from Methylobacterium extorquens AM1. J. Biol. Chem. 273:1998;25703-25712.
26. Sun D., Davidson V.L. Inter-subunit cross-linking of methylamine dehydrogenase by cyclopropylamine requires residue αPhe55. FEBS Lett. 517:2002;172-174.