EC Number   |
Metals/Ions |
Reference |
|---|
   1.7.5.1 | Fe |
complete coordination of the four Fe-S centers of the beta-subunit from Escherichia coli nitrate reductase |
696187 |
| 1.7.5.1 | Fe |
coordination model for the four [Fe-S] centres of the electron-transfer subunit NarH, coordination scheme of the [Fe-S] clusters, functional role of [Fe-S] centres |
697207 |
| 1.7.5.1 | Fe |
cysteine arrangements typical of iron-sulfur centers are found in the NarH polypeptide. This suggests that the latter is an electron transfer unit of the nitrate reductase complex |
700218 |
| 1.7.5.1 | Fe |
domain I of subunit NarG holds the [4Fe-4S] cluster FS0. The coordination scheme of FS0 is: His50, Cys54, Cys58, Cys93. NarH contains three [4Fe-4S] clusters, FS1, FS2, FS3 and one [3Fe-4S] cluster, FS4 |
700372 |
| 1.7.5.1 | Fe |
domain I of the catalytic subunit NadG holds the [4Fe-4S] cluster FS0 |
700372 |
| 1.7.5.1 | Fe |
several ironsulfur clusters |
672331 |
| 1.7.5.1 | Fe |
the 230000 Da complex contains 13 atoms iron and 12 atoms labile sulfur/molecules |
697691 |
| 1.7.5.1 | Fe |
the catalytic subunit of Escherichia coli nitrate reductase A contains a [4Fe-4S] cluster with a high-spin ground state |
658071 |
| 1.7.5.1 | Fe |
the four iron-sulfur centers of nitrate reductase A belong to two classes with markedly different redox potentials. The high-potential group comprises a [3Fe-4S] and a [4Fe-4S] cluster whose midpoint potentials are +60 mV and +80 mV, respectively. Although these centers are magnetically isolated, they are coupled by a significant anticooperative redox interaction of about 50 mV. The [4Fe-4S]1+ center occurs in two different conformations as shown by its composite EPR spectrum. The low-potential group contains two [4Fe-4S] clusters with more typical redox potentials (-200 mV and -400 mV). In the fully reduced state, the three [4Fe-4S]1+ centers are magnetically coupled. The iron-sulfur centers nitrate reductase Z and nitrate reductase A, exhibit essentially the same characteristics, except that the midpoint potentials of the high-potential centers of nitrate reductase Z appear negatively shifted by about 100 mV. A correspondence between the high-potential iron-sulfur clusters of the two enzymes can be proposed |
697693 |
| 1.7.5.1 | Fe2+ |
the enzyme binds one [4Fe-4S] cluster per subunit |
742333 |
