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Mutation of alphaPhe55 of methylamine dehydrogenase alters the reorganization energy and electronic coupling for its electron transfer reaction with amicyanin.

Sun D, Chen ZW, Mathews FS, Davidson VL
Biochemistry 41 13926-33 (2002)
Related entries: 1mg2, 2mta

Cited: 15 times
EuropePMC logo PMID: 12437349

Abstract

Methylamine dehydrogenase (MADH) possesses an alpha(2)beta(2) structure with each smaller beta subunit possessing a tryptophan tryptophylquinone (TTQ) prosthetic group. Phe55 of the alpha subunit is located where the substrate channel from the enzyme surface opens into the active site. Site-directed mutagenesis of alphaPhe55 has revealed roles for this residue in determining substrate specificity and binding monovalent cations at the active site. It is now shown that the alphaF55A mutation also increases the rate of the true electron transfer (ET) reaction from O-quinol MADH to amicyanin. The reorganization energy associated with the ET reaction is decreased from 2.3 to 1.8 eV. The electronic coupling associated with the ET reaction is decreased from 12 to 3 cm(-1). The crystal structure of alphaF55A MADH in complex with its electron acceptors, amicyanin and cytochrome c-551i, has been determined. Little difference in the overall structure is seen, relative to the native complex; however, there are significant changes in the solvent content of the active site and substrate channel. The crystal structure of alphaF55A MADH has also been determined with phenylhydrazine covalently bound to TTQ in the active site. Phenylhydrazine binding significantly perturbs the orientation of the TTQ rings relative to each other. The ET results are discussed in the context of the new and old crystal structures of the native and mutant enzymes.

Reviews - 1mg3 mentioned but not cited (1)

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Reviews citing this publication (4)

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  2. Electron transfer in quinoproteins. Davidson VL. Arch Biochem Biophys 428 32-40 (2004)
  3. Structure and mechanism of tryptophylquinone enzymes. Davidson VL. Bioorg Chem 33 159-170 (2005)
  4. Mechanisms for control of biological electron transfer reactions. Williamson HR, Dow BA, Davidson VL. Bioorg Chem 57 213-221 (2014)

Articles citing this publication (10)

  1. Protein control of true, gated, and coupled electron transfer reactions. Davidson VL. Acc Chem Res 41 730-738 (2008)
  2. Characterization of electron tunneling and hole hopping reactions between different forms of MauG and methylamine dehydrogenase within a natural protein complex. Choi M, Shin S, Davidson VL. Biochemistry 51 6942-6949 (2012)
  3. L358P mutation on cytochrome P450cam simulates structural changes upon putidaredoxin binding: the structural changes trigger electron transfer to oxy-P450cam from electron donors. Tosha T, Yoshioka S, Ishimori K, Morishima I. J Biol Chem 279 42836-42843 (2004)
  4. Rate-promoting vibrations and coupled hydrogen-electron transfer reactions in the condensed phase: a model for enzymatic catalysis. Mincer JS, Schwartz SD. J Chem Phys 120 7755-7760 (2004)
  5. X-ray structure of methanol dehydrogenase from Paracoccus denitrificans and molecular modeling of its interactions with cytochrome c-551i. Xia ZX, Dai WW, He YN, White SA, Mathews FS, Davidson VL. J Biol Inorg Chem 8 843-854 (2003)
  6. Electron transfer in crystals of the binary and ternary complexes of methylamine dehydrogenase with amicyanin and cytochrome c551i as detected by EPR spectroscopy. Ferrari D, Di Valentin M, Carbonera D, Merli A, Chen ZW, Mathews FS, Davidson VL, Rossi GL. J Biol Inorg Chem 9 231-237 (2004)
  7. Electron transfer from cytochrome c to cupredoxins. Takayama SJ, Irie K, Tai H, Kawahara T, Hirota S, Takabe T, Alcaraz LA, Donaire A, Yamamoto Y. J Biol Inorg Chem 14 821-828 (2009)
  8. Correlation of rhombic distortion of the type 1 copper site of M98Q amicyanin with increased electron transfer reorganization energy. Ma JK, Mathews FS, Davidson VL. Biochemistry 46 8561-8568 (2007)
  9. An artificial electron donor supported catalytic cycle of Pseudomonas putida cytochrome P450cam. Prasad S, Murugan R, Mitra S. Biochem Biophys Res Commun 335 590-595 (2005)
  10. Active-Site Environmental Factors Customize the Photophysics of Photoenzymatic Old Yellow Enzymes. Kudisch B, Oblinsky DG, Black MJ, Zieleniewska A, Emmanuel MA, Rumbles G, Hyster TK, Scholes GD. J Phys Chem B 124 11236-11249 (2020)


Related citations provided by authors (1)

  1. Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i.. Chen L, Durley RC, Mathews FS, Davidson VL Science 264 86-90 (1994)

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