References
55
108. Pollegioni L, Porrini D, Molla G, Pilone MS (2000) Redox potentials and their pH dependence
of D-amino-acid oxidase of Rhodotorula gracilis and Trigonopsis variabilis. Eur J Biochem
267:6624–6632
109. Yamazaki S, Isawa K, Kano K, Ikeda T, Taketomo N, Kaneko T (2000) Ascorbate regeneration
by the reduced form of 2-amino-3-carboxy-1,4-naphthoquinone, a strong growth stimulator
for bifidobacteria. J. Agric. Food Chem. 48:5643–5648
110. Maeda H, Matsu-ura S, Senba T, Yamasaki S, Takai H, Yamauchi Y, Ohmori H (2000)
Resorufin as an electron acceptor in glucose oxidase-catalyzed oxidation of glucose. Chem
Pharm Bull 48:897–902
111. Yamazaki S, Kano K, Ikeda T, Iwasa K, Kaneko T (1998) Mechanistic study on the roles
of a bifidogenetic growth stimulator based on physicochemical characterization. Biochem
Biophys Acta 1425:516–526
112. Swenson RP, Krey GD (1994) Site-directed mutagenesis of tyrosine-98 in the flavodoxin
from desulfovibrio vulgaris (Hildenborough): regulation of oxidationreduction properties of
the bound FMN cofactor by aromatic solvent, and electrostatic interactions. Biochemistry
33:8505–8514
113. Stankovich MT, Schopfer LM, Massay V (1978) Determination of glucose oxidase oxidationreduction potentials and the oxygen reactivity of fully reduced and semiquinoid forms. J Biol
Chem 253:4971–4979
114. Kirstein D, Kirstein L, Scheller F, Borcherding H, Ronnenberg J, Diekman S, Steinrucke
P (1999) Amperometric nitrate biosensors on the basis of Pseudomonas stutzeri nitrate
reductase. J Electroanal Chem 474:43–51
115. Lacey ALD, Hatchikian EC, Volbeda A, Frey M, Fontecilla-Camps JC, Fernandez VM (1997)
Infrared-spectroelectrochemical characterization of the [NiFe] hydrogenase of Desulfovibrio
gigas. J Am Chem Soc 119:7181–7189
116. Weber (1961) In: Long C (ed) Biochemists’ handbook. Spon, London, p 81
117. Lowe HJ, Clark WM (1956) Studies on oxidation-reduction XXIV. Oxidation-reduction
potentials of flavin adenine dinucleotide. J Biol Chem 221:983–992
118. Wilson DF, Erecinska M, Dutton PL (1974) Thermodynamic relationships in mitochondrial
oxidative phosphorylation. Annu Rev Biophys Bioeng 3:203–230
119. Breyer B, Buchanan GS, Duewell H (1944) The reduction potentials of acridines, with
reference to their antiseptic activity. J Chem Soc 360–363
120. Burton K (1957) Free energy data of biological interest. Ergeb Psysio 49:275–298
121. Loach PA (1976) In: Fasman GD (ed) Handbook of biochemistry and molecular biology.
Physical and chemical data, 3rd edn., vol I. CRC, p 129
55
108. Pollegioni L, Porrini D, Molla G, Pilone MS (2000) Redox potentials and their pH dependence
of D-amino-acid oxidase of Rhodotorula gracilis and Trigonopsis variabilis. Eur J Biochem
267:6624–6632
109. Yamazaki S, Isawa K, Kano K, Ikeda T, Taketomo N, Kaneko T (2000) Ascorbate regeneration
by the reduced form of 2-amino-3-carboxy-1,4-naphthoquinone, a strong growth stimulator
for bifidobacteria. J. Agric. Food Chem. 48:5643–5648
110. Maeda H, Matsu-ura S, Senba T, Yamasaki S, Takai H, Yamauchi Y, Ohmori H (2000)
Resorufin as an electron acceptor in glucose oxidase-catalyzed oxidation of glucose. Chem
Pharm Bull 48:897–902
111. Yamazaki S, Kano K, Ikeda T, Iwasa K, Kaneko T (1998) Mechanistic study on the roles
of a bifidogenetic growth stimulator based on physicochemical characterization. Biochem
Biophys Acta 1425:516–526
112. Swenson RP, Krey GD (1994) Site-directed mutagenesis of tyrosine-98 in the flavodoxin
from desulfovibrio vulgaris (Hildenborough): regulation of oxidationreduction properties of
the bound FMN cofactor by aromatic solvent, and electrostatic interactions. Biochemistry
33:8505–8514
113. Stankovich MT, Schopfer LM, Massay V (1978) Determination of glucose oxidase oxidationreduction potentials and the oxygen reactivity of fully reduced and semiquinoid forms. J Biol
Chem 253:4971–4979
114. Kirstein D, Kirstein L, Scheller F, Borcherding H, Ronnenberg J, Diekman S, Steinrucke
P (1999) Amperometric nitrate biosensors on the basis of Pseudomonas stutzeri nitrate
reductase. J Electroanal Chem 474:43–51
115. Lacey ALD, Hatchikian EC, Volbeda A, Frey M, Fontecilla-Camps JC, Fernandez VM (1997)
Infrared-spectroelectrochemical characterization of the [NiFe] hydrogenase of Desulfovibrio
gigas. J Am Chem Soc 119:7181–7189
116. Weber (1961) In: Long C (ed) Biochemists’ handbook. Spon, London, p 81
117. Lowe HJ, Clark WM (1956) Studies on oxidation-reduction XXIV. Oxidation-reduction
potentials of flavin adenine dinucleotide. J Biol Chem 221:983–992
118. Wilson DF, Erecinska M, Dutton PL (1974) Thermodynamic relationships in mitochondrial
oxidative phosphorylation. Annu Rev Biophys Bioeng 3:203–230
119. Breyer B, Buchanan GS, Duewell H (1944) The reduction potentials of acridines, with
reference to their antiseptic activity. J Chem Soc 360–363
120. Burton K (1957) Free energy data of biological interest. Ergeb Psysio 49:275–298
121. Loach PA (1976) In: Fasman GD (ed) Handbook of biochemistry and molecular biology.
Physical and chemical data, 3rd edn., vol I. CRC, p 129