Expression systems for soluble metal-dependent formate dehydrogenase
نویسندگان
چکیده
منابع مشابه
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...
متن کاملldentification 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...
متن کاملIdentification 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...
متن کاملKinetics for Formate Dehydrogenase of Escherichia coli
Kinetic parameters of the selenium-containing, formate dehydrogenase component of the Escherichia coli formate-hydrogenlyase complex have been determined with purified enzyme. A ping-pong Bi Bi kinetic mechanism was observed. The K,,, for formate is 26 mM, and the K,,, for the electron-accepting dye, benzyl viologen, is in the range 1-5 mM. The maximal turnover rate for the formate-dependent ca...
متن کاملFormate dehydrogenase from Ralstonia eutropha
1 Spectroscopic and kinetic properties of the molybdenum-containing, NAD+-dependent formate dehydrogenase from Ralstonia eutropha. Dimitri Niks, Jayant Duvvuru, Miguel Escalona, and Russ Hille Department of Biochemistry, University of California, Riverside, Riverside, CA 92521 Running title: Formate dehydrogenase from Ralstonia eutropha To whom correspondence should be addressed: Prof. Russ Hil...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Photochemistry and Photobiology A: Chemistry
سال: 2015
ISSN: 1010-6030
DOI: 10.1016/j.jphotochem.2015.06.028