NAD+-dependent formate dehydrogenase

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NAD + -dependent Formate Dehydrogenase from Plants

NAD(+)-dependent formate dehydrogenase (FDH, EC 1.2.1.2) widely occurs in nature. FDH consists of two identical subunits and contains neither prosthetic groups nor metal ions. This type of FDH was found in different microorganisms (including pathogenic ones), such as bacteria, yeasts, fungi, and plants. As opposed to microbiological FDHs functioning in cytoplasm, plant FDHs localize in mitochon...

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Efficient CO2-Reducing Activity of NAD-Dependent Formate Dehydrogenase from Thiobacillus sp. KNK65MA for Formate Production from CO2 Gas

NAD-dependent formate dehydrogenase (FDH) from Candida boidinii (CbFDH) has been widely used in various CO2-reduction systems but its practical applications are often impeded due to low CO2-reducing activity. In this study, we demonstrated superior CO2-reducing properties of FDH from Thiobacillus sp. KNK65MA (TsFDH) for production of formate from CO2 gas. To discover more efficient CO2-reducing...

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ldentification of a Maior Soluble Protein in Mitochondria from Nonphotosynthetic Tissues as NAD-Dependent Formate Dehydrogenase'

ase) (Douce and Neuburger, 1989). Gly is oxidized in the Of Gly decarboxylase and Ser hYdroxYmethY1transferase. This is an important ste?' in the process of photorespiration. The Gly cleavage system purified from plant mitochondria (Neuburger et al., 1986; Walker and Oliver, 1986) is composed of four subunits, P (94 kD), L (60 kD), T (41 kD), and H (15 kD). This complex is very abundant in gree...

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Effect of pH on kinetic parameters of NAD+-dependent formate dehydrogenase.

To define in detail the molecular mechanism of NAD+-dependent formate dehydrogenase, the pH dependences of various kinetic and spectroscopic parameters have been studied: Vmax, Km (NAD+), Km (formate), inhibition constants for structural analogues of substrate (NO3-) and product (CNS-, CNO-, N3-), CD and fluorescence properties. The value of Vmax, rate-limiting hydride transfer, is nearly const...

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Identification of a major soluble protein in mitochondria from nonphotosynthetic tissues as NAD-dependent formate dehydrogenase.

In many plant species, one of the most abundant soluble proteins (as judged by two-dimensional polyacrylamide gel electrophoresis) in mitochondria from nongreen tissues is a 40-kD polypeptide that is relatively scarce in mitochondria from photosynthetic tissues. cDNA sequences encoding this polypeptide were isolated from a lambda gt11 cDNA expression library from potato (Solanum tuberosum L.) b...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1994

ISSN: 0264-6021,1470-8728

DOI: 10.1042/bj3010625