References
21
22. Fujieda N, Mori M, Ikeda T, Kano K (2009) The silent form of quinohemoprotein amine
dehydrogenase from paracoccus denitrificans. Biosci Biotechnol Biochem 73:524–529
23. Kano K, Mori K, Uno B, Kubota T, Ikeda T, Senda M (1990) Voltammetric determination
of acid dissociation constants of pyrroloquinoline quinone and its reduced form under acidic
conditions. Bioelectrochem Bioenerg 24:193–201
24. Kano K, Mori K, Uno B, Goto M (1990) Voltammetric and spectroscopic properties of the
ammonia adduct of pyrroloquinoline quinone. J Electroanal Chem 293:177–184
25. Kano K, Mori T, Uno B, Goto M, Ikeda T (1993) Characterization of topa quinone cofactor.
Biochim Biophys Acta 1157:324–331
26. Itoh S, Ogino M, Haranou S, Terasaka T, Ando T, Komatsu M, Ohshiro Y, Fukuzumi S, Kano K,
Takagi K, Ikeda T (1995) A model compound of novel cofactor tryptophan tryptophylquinone
of bacterial methylamine dehydrogenases. Synthesis and physicochemical properties. J Am
Chem Soc 117:1485–1493
27. Murakami Y, Yoshimoto N, Fujieda N, Ohkubo K, Hasegawa T, Kano K, Fukuzumi S,
Itoh S (2007) Model studies of 6,7-indolequinone cofactors of quinohemoprotein amine
dehydrogenases. J Org Chem 72:3369–3380
28. Sato A, Takagi K, Kano K, Kato N, Duine JA, Ikeda T (2001) Ca 2+ stabilizes the semiquinone
radical of pyrroloquinoline quinone. Biochem J 357:893–898
29. Fujieda N, Mori M, Kano K, Ikeda T (2002) Spectroelectrochemical evaluation of redox potentials of cysteine tryptophylquinone and two hemes c in quinohemoprotein amine dehydrogenase
from Paracoccus denitrificans. Biochemistry 41:13736–13743
30. Dunford HB (1998) Heme enzymes. In: Sinnot M (ed) Comprehensive biological catalysis (a
mechanistic reference), vol III, Chap 32. Academic Press, London
31. Harel A, Bromberg Y, Falkowski PG, Bhattacharya D (2014) Evolutionary history of redox
metal-binding domains across the tree of life. Proc Natl Acad Sci USA 111:7042–7047
32. Wuttle DS, Gray HB (1993) Protein engineering as a tool for understanding electron transfer.
Curr Opin Struct Biol 3:555–563
33. Messerschmidt A (1998) Copper metalloenzymes. In: Sinnot M (ed) Comprehensive biological
catalysis (a mechanistic reference), vol III, Chap 38. Academic Press, London
34. Tsujimura S, Kuriyama A, Fujieda N, Kano K, Ikeda T (2005) Mediated spectroelectrochemical
titration of proteins for redox potential measurements by a separator-less one-compartment bulk
electrolysis method. Anal Biochem 337:325–331
35. Reinhammar BRM (1972) Oxidation-reduction potentials of the electron acceptors in laccases
and stellacyanin. Biochim Biophys Acta 275:245–259
36. Kamitaka Y, Tsujimura S, Kataoka K, Sakurai T, Ikeda T, Kano K (2007) Effects of axial
ligand mutation of the type I copper site in bilirubin oxidase on direct electron transfer-type
bioelectrocatalytic reduction of dioxygen. J Electroanal Chem 601:119–124
37. Kurose S, Kataoka K, Shinohara N, Miura Y, Tsutsumi M, Tsujimura S, Kano K, Sakurai T
(2009) Modification of spectroscopic properties and catalytic activity of escherichia coli CueO
by mutations of methionine 510, the axial ligand to type I Cu. Bull Chem Soc Jpn 82:504–508
38. Durã P, Chen Z, Silva CS, Soares CM, Pereira MM, Todorovic S, Hildebrandt P, Bento I,
Lindley PF, Martins LO (2008) Proximal mutations at the type 1 copper site of CotA laccase:
spectroscopic, redox, kinetic and structural characterization of I494A and L386A mutants.
Biochem J 412:339–346
39. Halcrow MA (1998) Nickel-dependent redox enzymes. In: Sinnot M (ed) Comprehensive
biological catalysis (a mechanistic reference), vol III, Chap 38. Academic Press, London
40. Ogata H, Lubits W, Higuchi Y (2016) Structure and function of [NiFe] hydrogenase. J Biochem
160:251–258
41. Baugh PE, Collison D, Garner CD, Joule JA (1998) Molybdenum metalloenzymes. In: Sinnot M
(ed) comprehensive biological catalysis (a mechanistic reference), vol III, Chap 38. Academic
Press, London
42. Barton SC, Gallaway J, Atanassov P (2004) Enzymatic biofuel cells for implantable and
microscale devices. Chem Rev 104:4867–4886
43. Heller A Potentially implantable miniature batteries. Anal Bioanal Chem 385, f
21
22. Fujieda N, Mori M, Ikeda T, Kano K (2009) The silent form of quinohemoprotein amine
dehydrogenase from paracoccus denitrificans. Biosci Biotechnol Biochem 73:524–529
23. Kano K, Mori K, Uno B, Kubota T, Ikeda T, Senda M (1990) Voltammetric determination
of acid dissociation constants of pyrroloquinoline quinone and its reduced form under acidic
conditions. Bioelectrochem Bioenerg 24:193–201
24. Kano K, Mori K, Uno B, Goto M (1990) Voltammetric and spectroscopic properties of the
ammonia adduct of pyrroloquinoline quinone. J Electroanal Chem 293:177–184
25. Kano K, Mori T, Uno B, Goto M, Ikeda T (1993) Characterization of topa quinone cofactor.
Biochim Biophys Acta 1157:324–331
26. Itoh S, Ogino M, Haranou S, Terasaka T, Ando T, Komatsu M, Ohshiro Y, Fukuzumi S, Kano K,
Takagi K, Ikeda T (1995) A model compound of novel cofactor tryptophan tryptophylquinone
of bacterial methylamine dehydrogenases. Synthesis and physicochemical properties. J Am
Chem Soc 117:1485–1493
27. Murakami Y, Yoshimoto N, Fujieda N, Ohkubo K, Hasegawa T, Kano K, Fukuzumi S,
Itoh S (2007) Model studies of 6,7-indolequinone cofactors of quinohemoprotein amine
dehydrogenases. J Org Chem 72:3369–3380
28. Sato A, Takagi K, Kano K, Kato N, Duine JA, Ikeda T (2001) Ca 2+ stabilizes the semiquinone
radical of pyrroloquinoline quinone. Biochem J 357:893–898
29. Fujieda N, Mori M, Kano K, Ikeda T (2002) Spectroelectrochemical evaluation of redox potentials of cysteine tryptophylquinone and two hemes c in quinohemoprotein amine dehydrogenase
from Paracoccus denitrificans. Biochemistry 41:13736–13743
30. Dunford HB (1998) Heme enzymes. In: Sinnot M (ed) Comprehensive biological catalysis (a
mechanistic reference), vol III, Chap 32. Academic Press, London
31. Harel A, Bromberg Y, Falkowski PG, Bhattacharya D (2014) Evolutionary history of redox
metal-binding domains across the tree of life. Proc Natl Acad Sci USA 111:7042–7047
32. Wuttle DS, Gray HB (1993) Protein engineering as a tool for understanding electron transfer.
Curr Opin Struct Biol 3:555–563
33. Messerschmidt A (1998) Copper metalloenzymes. In: Sinnot M (ed) Comprehensive biological
catalysis (a mechanistic reference), vol III, Chap 38. Academic Press, London
34. Tsujimura S, Kuriyama A, Fujieda N, Kano K, Ikeda T (2005) Mediated spectroelectrochemical
titration of proteins for redox potential measurements by a separator-less one-compartment bulk
electrolysis method. Anal Biochem 337:325–331
35. Reinhammar BRM (1972) Oxidation-reduction potentials of the electron acceptors in laccases
and stellacyanin. Biochim Biophys Acta 275:245–259
36. Kamitaka Y, Tsujimura S, Kataoka K, Sakurai T, Ikeda T, Kano K (2007) Effects of axial
ligand mutation of the type I copper site in bilirubin oxidase on direct electron transfer-type
bioelectrocatalytic reduction of dioxygen. J Electroanal Chem 601:119–124
37. Kurose S, Kataoka K, Shinohara N, Miura Y, Tsutsumi M, Tsujimura S, Kano K, Sakurai T
(2009) Modification of spectroscopic properties and catalytic activity of escherichia coli CueO
by mutations of methionine 510, the axial ligand to type I Cu. Bull Chem Soc Jpn 82:504–508
38. Durã P, Chen Z, Silva CS, Soares CM, Pereira MM, Todorovic S, Hildebrandt P, Bento I,
Lindley PF, Martins LO (2008) Proximal mutations at the type 1 copper site of CotA laccase:
spectroscopic, redox, kinetic and structural characterization of I494A and L386A mutants.
Biochem J 412:339–346
39. Halcrow MA (1998) Nickel-dependent redox enzymes. In: Sinnot M (ed) Comprehensive
biological catalysis (a mechanistic reference), vol III, Chap 38. Academic Press, London
40. Ogata H, Lubits W, Higuchi Y (2016) Structure and function of [NiFe] hydrogenase. J Biochem
160:251–258
41. Baugh PE, Collison D, Garner CD, Joule JA (1998) Molybdenum metalloenzymes. In: Sinnot M
(ed) comprehensive biological catalysis (a mechanistic reference), vol III, Chap 38. Academic
Press, London
42. Barton SC, Gallaway J, Atanassov P (2004) Enzymatic biofuel cells for implantable and
microscale devices. Chem Rev 104:4867–4886
43. Heller A Potentially implantable miniature batteries. Anal Bioanal Chem 385, f