Deyhle R R, Barton L L
Can J Microbiol. 1977 Feb;23(2):125-30. doi: 10.1139/m77-018.
Formate dehydrogenase activity (EC 1.2.1.2) has been demonstrated in cell-free preparations of Mycobacterium phlei by following the reduction of 2,6 dichlorophenolindophenol. thiazolyl blue tetrazolium, or equine cytochrome c. The reduction of equine cytochrome c was inhibited by 2-heptyl-4-hydroxyquinoline-N-oxide. Neither nicotinamide adenine dinucleotide nor nicotinamide adenine dinucleotide phosphate were reduced by this formate dehydrogenase. The enzyme was constitutive and associated with the particular fraction. The greatest level of activity was observed at pH 9.0, with 8 mM formate, and with extracts of cells taken from the log phase of growth. Formaldehyde, hypophosphite, nitrate, and bicarbonate all inhibited the oxidation of formate.
通过监测2,6-二氯酚靛酚、噻唑蓝四氮唑或马细胞色素c的还原反应，已在草分枝杆菌的无细胞制剂中证实了甲酸脱氢酶活性（EC 1.2.1.2）。马细胞色素c的还原反应受到2-庚基-4-羟基喹啉-N-氧化物的抑制。该甲酸脱氢酶既不还原烟酰胺腺嘌呤二核苷酸，也不还原烟酰胺腺嘌呤二核苷酸磷酸。该酶是组成型的，且与特定组分相关。在pH 9.0、8 mM甲酸盐以及取自对数生长期细胞的提取物存在的条件下，观察到了最高水平的活性。甲醛、次磷酸盐、硝酸盐和碳酸氢盐均抑制甲酸盐的氧化反应。
