TABLE 2.
Summary of NDH-2 biochemical features
| Organism | Group | Em | Km (μM) | Mm (kDa) | Flavin | QBS |
|---|---|---|---|---|---|---|
| E. coli | A | NDd | 50 | 45 | FAD | IB |
| A. vinelandii | A | ND | 13 | ND | FAD | IB |
| Synechocystis | A | ND | ND | 49c | FAD | IB |
| A. ambivalens | C | +70 | 6 | 47 | FMN | IA |
| S. metallicus | C | +160 | 2 | 49 | FMN | ND |
| T. brucei | A | ND | 120 | 2 × 33 | FMN | IC |
| Y. lipolytica | A | ND | 15 | 66c | FAD | IB |
| S. cerevisiae | ||||||
| NDI1 | A | −370 | 31, 9a | 53 | FAD | IA |
| NDE1 | A | ND | ND | 62c | FAD | IB |
| NDE2 | A | ND | ND | 65c | FAD | IB |
| N. crassa | ||||||
| NDI1 | A | ND | 57 | FAD | IB | |
| NDE1 | B | ND | 11b | 64 | FAD | IB |
| NDE2 | A | ND | 12 | 65c | FAD | IB |
| S. tuberosum | ||||||
| NDA | A | ND | 14b | 55c | FAD | IA |
| NDin | ND | ND | 14b | ND | FAD | ND |
| NDB | B | ND | ND | 65 | FAD | IC |
| NDex | ND | ND | ND | ND | FAD | ND |
a
Values obtained using Q6 or DCPIP, respectively.
b
The experiments were carried out with intact mitochondria (N. crassa) or inside-out submitochondrial particles (S. tuberosum); thus, the Km values stand for external or internal NAD(P)H dehydrogenases, respectively.
c
Estimated from the sequence of the precursor protein.
d
ND, not determined. Fingerprints of type 1 Quinone-Binding Sites (QBS): type IA L(X)3H(X)2T, type IB (A/L/I)(X)3H(X)2L, and type IC L(X)3H(X)3S.