155 related articles for article (PubMed ID: 11035020)
1. Heme ligation and conformational plasticity in the isolated c domain of cytochrome cd1 nitrite reductase.
Steensma E; Gordon E; Oster LM; Ferguson SJ; Hajdu J
J Biol Chem; 2001 Feb; 276(8):5846-55. PubMed ID: 11035020
[TBL] [Abstract][Full Text] [Related]
2. Structure and kinetic properties of Paracoccus pantotrophus cytochrome cd1 nitrite reductase with the d1 heme active site ligand tyrosine 25 replaced by serine.
Gordon EH; Sjögren T; Löfqvist M; Richter CD; Allen JW; Higham CW; Hajdu J; Fülöp V; Ferguson SJ
J Biol Chem; 2003 Apr; 278(14):11773-81. PubMed ID: 12556530
[TBL] [Abstract][Full Text] [Related]
3. A switch in heme axial ligation prepares Paracoccus pantotrophus cytochrome cd1 for catalysis.
Allen JW; Watmough NJ; Ferguson SJ
Nat Struct Biol; 2000 Oct; 7(10):885-8. PubMed ID: 11017198
[TBL] [Abstract][Full Text] [Related]
4. The cytochrome c domain of dimeric cytochrome cd(1) of Paracoccus pantotrophus can be produced at high levels as a monomeric holoprotein using an improved c-type cytochrome expression system in Escherichia coli.
Gordon EH; Steensma E; Ferguson SJ
Biochem Biophys Res Commun; 2001 Mar; 281(3):788-94. PubMed ID: 11237728
[TBL] [Abstract][Full Text] [Related]
5. X-ray crystallographic study of cyanide binding provides insights into the structure-function relationship for cytochrome cd1 nitrite reductase from Paracoccus pantotrophus.
Jafferji A; Allen JW; Ferguson SJ; Fulop V
J Biol Chem; 2000 Aug; 275(33):25089-94. PubMed ID: 10827177
[TBL] [Abstract][Full Text] [Related]
6. Activation of the cytochrome cd1 nitrite reductase from Paracoccus pantotrophus. Reaction of oxidized enzyme with substrate drives a ligand switch at heme c.
van Wonderen JH; Knight C; Oganesyan VS; George SJ; Zumft WG; Cheesman MR
J Biol Chem; 2007 Sep; 282(38):28207-15. PubMed ID: 17623666
[TBL] [Abstract][Full Text] [Related]
7. Two enzymes with a common function but different heme ligands in the forms as isolated. Optical and magnetic properties of the heme groups in the oxidized forms of nitrite reductase, cytochrome cd1, from Pseudomonas stutzeri and Thiosphaera pantotropha.
Cheesman MR; Ferguson SJ; Moir JW; Richardson DJ; Zumft WG; Thomson AJ
Biochemistry; 1997 Dec; 36(51):16267-76. PubMed ID: 9405061
[TBL] [Abstract][Full Text] [Related]
8. The Structure of an alternative form of Paracoccus pantotrophus cytochrome cd(1) nitrite reductase.
Sjögren T; Hajdu J
J Biol Chem; 2001 Aug; 276(31):29450-5. PubMed ID: 11373294
[TBL] [Abstract][Full Text] [Related]
9. Probing the unusual oxidation/reduction behavior of Paracoccus pantotrophus cytochrome cd1 nitrite reductase by replacing a switchable methionine heme iron ligand with histidine.
Zajicek RS; Cartron ML; Ferguson SJ
Biochemistry; 2006 Sep; 45(37):11208-16. PubMed ID: 16964982
[TBL] [Abstract][Full Text] [Related]
10. Y25S variant of Paracoccus pantotrophus cytochrome cd1 provides insight into anion binding by d1 heme and a rare example of a critical difference between solution and crystal structures.
Zajicek RS; Cheesman MR; Gordon EH; Ferguson SJ
J Biol Chem; 2005 Jul; 280(28):26073-9. PubMed ID: 15901734
[TBL] [Abstract][Full Text] [Related]
11. A novel, kinetically stable, catalytically active, all-ferric, nitrite-bound complex of Paracoccus pantotrophus cytochrome cd1.
Allen JW; Higham CW; Zajicek RS; Watmough NJ; Ferguson SJ
Biochem J; 2002 Sep; 366(Pt 3):883-8. PubMed ID: 12086580
[TBL] [Abstract][Full Text] [Related]
12. Paracoccus pantotrophus NapC can reductively activate cytochrome cd1 nitrite reductase.
Zajicek RS; Allen JW; Cartron ML; Richardson DJ; Ferguson SJ
FEBS Lett; 2004 May; 565(1-3):48-52. PubMed ID: 15135051
[TBL] [Abstract][Full Text] [Related]
13. Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme.
Williams PA; Fülöp V; Garman EF; Saunders NF; Ferguson SJ; Hajdu J
Nature; 1997 Sep; 389(6649):406-12. PubMed ID: 9311786
[TBL] [Abstract][Full Text] [Related]
14. A novel conformer of oxidized Paracoccus pantotrophus cytochrome cd(1) observed by freeze-quench NIR-MCD spectroscopy.
Allen JW; Cheesman MR; Higham CW; Ferguson SJ; Watmough NJ
Biochem Biophys Res Commun; 2000 Dec; 279(2):674-7. PubMed ID: 11118344
[TBL] [Abstract][Full Text] [Related]
15. Proton-coupled structural changes upon binding of carbon monoxide to cytochrome cd1: a combined flash photolysis and X-ray crystallography study.
Sjögren T; Svensson-Ek M; Hajdu J; Brzezinski P
Biochemistry; 2000 Sep; 39(36):10967-74. PubMed ID: 10998233
[TBL] [Abstract][Full Text] [Related]
16. Structure of the bound dioxygen species in the cytochrome oxidase reaction of cytochrome cd1 nitrite reductase.
Sjögren T; Hajdu J
J Biol Chem; 2001 Apr; 276(16):13072-6. PubMed ID: 11278884
[TBL] [Abstract][Full Text] [Related]
17. Quantum mechanical interpretation of nitrite reduction by cytochrome cd1 nitrite reductase from Paracoccus pantotrophus.
Ranghino G; Scorza E; Sjögren T; Williams PA; Ricci M; Hajdu J
Biochemistry; 2000 Sep; 39(36):10958-66. PubMed ID: 10998232
[TBL] [Abstract][Full Text] [Related]
18. Conformational changes occurring upon reduction and NO binding in nitrite reductase from Pseudomonas aeruginosa.
Nurizzo D; Cutruzzolà F; Arese M; Bourgeois D; Brunori M; Cambillau C; Tegoni M
Biochemistry; 1998 Oct; 37(40):13987-96. PubMed ID: 9760233
[TBL] [Abstract][Full Text] [Related]
19. Oxidase reaction of cytochrome cd(1) from Paracoccus pantotrophus.
Koppenhöfer A; Little RH; Lowe DJ; Ferguson SJ; Watmough NJ
Biochemistry; 2000 Apr; 39(14):4028-36. PubMed ID: 10747791
[TBL] [Abstract][Full Text] [Related]
20. Magnetic circular dichroism evidence for a weakly coupled heme-radical pair at the active site of cytochrome cd1, a nitrite reductase.
Oganesyan VS; Cheesman MR; Thomson AJ
Inorg Chem; 2007 Dec; 46(26):10950-2. PubMed ID: 18044879
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
