| 别名 |
bchB, bchL, bchN, ChlB, ChlL, ChlN, dark operative protochlorophyllide oxidoreductase, dark protochlorophyllide reductase, dark-operative DPOR, dark-operative Pchlide oxidoreductase, dark-operative protochlorophyllide oxidoreductase, dark-operative protochlorophyllide reductase, DPOR, light-independent (dark) Pchlide reductase, light-independent (dark-operative) Pchlide oxidoreductase, light-independent Pchlide oxidoreductase, light-independent Pchlide reductase, light-independent protochlorophyllide oxidoreductase, light-independent protochlorophyllide oxidoreductases, light-independent protochlorophyllide reductase, LIPOR, PORA, protochlorophyllide oxidoreductase, protochlorophyllide oxidoreductase complex |
| Comments |
Occurs in photosynthetic bacteria, cyanobacteria, green algae and gymnosperms. The enzyme catalyses trans-reduction of the D-ring of protochlorophyllide; the product has the (7S,8S)-configuration. Unlike EC 1.3.1.33 (protochlorophyllide reductase), light is not required. The enzyme contains a [4Fe-4S] cluster, and structurally resembles the Fe protein/MoFe protein complex of nitrogenase (EC 1.18.6.1), which catalyses an ATP-driven reduction. |
