20
1 Redox Proteins and Bioelectrocatalysis
References
1. Bugg TDH (2014) Introduction to enzyme and coenzyme chemistry, 2nd edn, Chap 6. Blackwell
Publishing, Oxford
2. Sinnot M (1998) Comprehensive biological catalysis (a mechanistic reference), vol III, Chap
28. Academic Press, London
3. Falkowski PG, Fenchel T, Delong EF (2008) The microbial engines that drive earth’s
biogeochemical cycles. Science 320:1034–1039
4. https://www.qmul.ac.uk/sbcs/iubmb/enzyme/
5. Clark AR, Dafforn TR (1998) NAD + and NADP-linked reactions. In: Sinnot M (ed) Comprehensive biological catalysis (a mechanistic reference), vol III, Chap 28. Academic Press,
London
6. Palfey BA, Massey V (1998) Flavin-dependent enzymes. In: Sinnot EM (ed) Comprehensive
biological catalysis (a mechanistic reference), vol III, Chap 29. Academic Press, London
7. Bartlett PN (2008) Bioelectrochemistry (fundamentals, experimental techniques and applications). Wiley
8. Edmondson DE, Francesco RD (1991) Muller F (ed) Chemistry and biochemistry of
flavoenzymes. CRC Press, Boca Raton, pp 73–103
9. Decker KF (1993) Biosynthesis and function of enzymes with covalently bound flavin. Annu
Rev Nutr 13:17–41
10. Fujieda N, Satoh A, Tsuse N, Kano K, Ikeda T (2004) 6-S-cysteinyl flavin mononucleotidecontaining histamine dehydrogenase from Nocardioides simplex: molecular cloning,
sequencing, over-expression and characterization of redox centers of enzyme. Biochemistry
43:10800–10808
11. Tatsumi H, Nakase H, Kano K, Ikeda T (1998) Mechanistic study of the autoxidation of reduced
flavin and quinone compounds. J Electroanal Chem 443:236–242
12. Anthony C (1998) Quinoprotein-catalyzed reactions. In: Sinnot M (1998) Comprehensive
biological catalysis (a mechanistic reference), vol III, Chap 30. Academic Press, London (1998)
13. Westerling J, Frank J, Duine FA (1979) The prosthetic group of methanol dehydrogenase
from Hyphomicrobium X: electron spin resonance evidence for a quinone structure. Biochem
Biophys Res Commun 87:719–724
14. Salisbury SA, Forrest HS, Cruse WBT, Kennard O (1979) A novel coenzyme from bacterial
primary alcohol dehydrogenases. Nature 280:843–844
15. Kano K, Mori K, Uno B, Kubota T, Ikeda T, Senda M (1990) Voltammetric and spectroscopic studies of pyrroloquinoline quinone coenzyme under neutral and basic conditions.
Bioelectrochem Bioenerg 23:227–238
16. Janes SM, Mu D, Wemmer D, Smith AJ, Kaur S, Maltby D, Burlingame AL, Klinman JP (1990)
A new redox cofactor in eukaryotic enzymes: 6-hydroxydopa at the active site of bovine serum
amine oxidase. Science 248:981–987
17. McIntire WS, Wemmer DE, Chistoserdov A, Lidstrom ME (1991) A new cofactor in a prokaryotic enzyme: tryptophan tryptophylquinone as the redox prosthetic group in methylamine
dehydrogenase. Science 252:817–824
18. Wang S-X, Mure M, Medzihradszky KF, Burlingame AL, Brown DE, Dooley DM, Smith AJ,
Kagan HM, Klinman JP (1996) A crosslinked cofactor in lysyl oxidase: redox function for
amino acid side chains. Science 273:1078–1084
19. Datta S, Mori Y, Takagi Y, Kawaguchi Z-W, Okajima CT, Kuroda S, Ikeda T, Kano K,
Tanizawa K, Mathews FS (2001) Structure of a quinohemoprotein amine dehydrogenase with
an uncommon redox cofactor and highly unusual crosslinking. Proc Natl Acad Sci, USA
98:14268–14273
20. van Kleef MAG, Jongejan JA, Duine JA (1989) Factors relevant in the reaction of pyrroloquinoline quinone with amino acids. Eur J Biochem 183:43–47
21. Esaka Y, Goto YM, Kano K (1994) Kinetic analysis of oxalopyrroloquinoline formation in the
reaction of coenzyme PQQ with amino acids by capillary zone electrophoresis. J Chem Soc
Perkin Trans 2:2163–2167
1 Redox Proteins and Bioelectrocatalysis
References
1. Bugg TDH (2014) Introduction to enzyme and coenzyme chemistry, 2nd edn, Chap 6. Blackwell
Publishing, Oxford
2. Sinnot M (1998) Comprehensive biological catalysis (a mechanistic reference), vol III, Chap
28. Academic Press, London
3. Falkowski PG, Fenchel T, Delong EF (2008) The microbial engines that drive earth’s
biogeochemical cycles. Science 320:1034–1039
4. https://www.qmul.ac.uk/sbcs/iubmb/enzyme/
5. Clark AR, Dafforn TR (1998) NAD + and NADP-linked reactions. In: Sinnot M (ed) Comprehensive biological catalysis (a mechanistic reference), vol III, Chap 28. Academic Press,
London
6. Palfey BA, Massey V (1998) Flavin-dependent enzymes. In: Sinnot EM (ed) Comprehensive
biological catalysis (a mechanistic reference), vol III, Chap 29. Academic Press, London
7. Bartlett PN (2008) Bioelectrochemistry (fundamentals, experimental techniques and applications). Wiley
8. Edmondson DE, Francesco RD (1991) Muller F (ed) Chemistry and biochemistry of
flavoenzymes. CRC Press, Boca Raton, pp 73–103
9. Decker KF (1993) Biosynthesis and function of enzymes with covalently bound flavin. Annu
Rev Nutr 13:17–41
10. Fujieda N, Satoh A, Tsuse N, Kano K, Ikeda T (2004) 6-S-cysteinyl flavin mononucleotidecontaining histamine dehydrogenase from Nocardioides simplex: molecular cloning,
sequencing, over-expression and characterization of redox centers of enzyme. Biochemistry
43:10800–10808
11. Tatsumi H, Nakase H, Kano K, Ikeda T (1998) Mechanistic study of the autoxidation of reduced
flavin and quinone compounds. J Electroanal Chem 443:236–242
12. Anthony C (1998) Quinoprotein-catalyzed reactions. In: Sinnot M (1998) Comprehensive
biological catalysis (a mechanistic reference), vol III, Chap 30. Academic Press, London (1998)
13. Westerling J, Frank J, Duine FA (1979) The prosthetic group of methanol dehydrogenase
from Hyphomicrobium X: electron spin resonance evidence for a quinone structure. Biochem
Biophys Res Commun 87:719–724
14. Salisbury SA, Forrest HS, Cruse WBT, Kennard O (1979) A novel coenzyme from bacterial
primary alcohol dehydrogenases. Nature 280:843–844
15. Kano K, Mori K, Uno B, Kubota T, Ikeda T, Senda M (1990) Voltammetric and spectroscopic studies of pyrroloquinoline quinone coenzyme under neutral and basic conditions.
Bioelectrochem Bioenerg 23:227–238
16. Janes SM, Mu D, Wemmer D, Smith AJ, Kaur S, Maltby D, Burlingame AL, Klinman JP (1990)
A new redox cofactor in eukaryotic enzymes: 6-hydroxydopa at the active site of bovine serum
amine oxidase. Science 248:981–987
17. McIntire WS, Wemmer DE, Chistoserdov A, Lidstrom ME (1991) A new cofactor in a prokaryotic enzyme: tryptophan tryptophylquinone as the redox prosthetic group in methylamine
dehydrogenase. Science 252:817–824
18. Wang S-X, Mure M, Medzihradszky KF, Burlingame AL, Brown DE, Dooley DM, Smith AJ,
Kagan HM, Klinman JP (1996) A crosslinked cofactor in lysyl oxidase: redox function for
amino acid side chains. Science 273:1078–1084
19. Datta S, Mori Y, Takagi Y, Kawaguchi Z-W, Okajima CT, Kuroda S, Ikeda T, Kano K,
Tanizawa K, Mathews FS (2001) Structure of a quinohemoprotein amine dehydrogenase with
an uncommon redox cofactor and highly unusual crosslinking. Proc Natl Acad Sci, USA
98:14268–14273
20. van Kleef MAG, Jongejan JA, Duine JA (1989) Factors relevant in the reaction of pyrroloquinoline quinone with amino acids. Eur J Biochem 183:43–47
21. Esaka Y, Goto YM, Kano K (1994) Kinetic analysis of oxalopyrroloquinoline formation in the
reaction of coenzyme PQQ with amino acids by capillary zone electrophoresis. J Chem Soc
Perkin Trans 2:2163–2167