In enzymology, a D-lactate dehydrogenase (cytochrome) (EC 1.1.2.4) is an enzyme that catalyzes the chemical reaction

(D)-lactate + 2 ferricytochrome c ${\displaystyle \rightleftharpoons }$ pyruvate + 2 ferrocytochrome c

Thus, the two substrates of this enzyme are (D)-lactate and ferricytochrome c, whereas its two products are pyruvate and ferrocytochrome c.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is (D)-lactate:ferricytochrome-c 2-oxidoreductase. Other names in common use include lactic acid dehydrogenase, D-lactate (cytochrome) dehydrogenase, cytochrome-dependent D-(−)-lactate dehydrogenase, D-lactate-cytochrome c reductase, and D-(−)-lactic cytochrome c reductase. This enzyme participates in pyruvate metabolism. It employs one cofactor, FAD. This type of enzyme has been characterized in animals, fungi, bacteria and recently in plants^[1] .^[2] It is believed to be important in the detoxification of methylglyoxal through the glyoxylase pathway

• GREGOLIN C, SINGER TP (1963). "The lactic dehydrogenase of yeast. III. D(-)Lactic cytochrome c reductase, a zinc-flavoprotein from aerobic yeast". Biochim. Biophys. Acta. 67: 201–18. doi:10.1016/0006-3002(63)91818-3. PMID 13950255.
• GREGOLIN C, SINGER TP, KEARNEY EB, BOERI E (1961). "The formation and enzymatic properties of the various lactic dehydrogenases of yeast". Ann. N. Y. Acad. Sci. 94 (3): 780–97. Bibcode:1961NYASA..94..780G. doi:10.1111/j.1749-6632.1961.tb35573.x. PMID 13901630.
• Nygaard AP (1961). "D(−)-Lactate cytochrome c reductase, a flavoprotein from yeast". J. Biol. Chem. 236 (3): 920–925. doi:10.1016/S0021-9258(18)64331-5. PMID 13729965.
• Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 557-565.