PMID- 15125645
OWN - NLM
STAT- MEDLINE
DCOM- 20040728
LR  - 20080117
IS  - 0002-7863 (Print)
IS  - 0002-7863 (Linking)
VI  - 126
IP  - 18
DP  - 2004 May 12
TI  - Mapping of the binding site on pseudoazurin in the transient 152 kDa complex with 
      nitrite reductase.
PG  - 5658-9
AB  - Nitrite reductase (NiR) catalyzes the reduction of nitrite to nitrite oxide as a 
      part of the denitrification process. In Alcaligenes faecalis S-6, the copper 
      protein pseudoazurin acts as electron donor to NiR. The binding surface of 
      pseudoazurin involved in the formation of the 152 kDa complex with NiR has been 
      determined by NMR using cross saturation from NiR to perdeuterated pseudoazurin. 
      Due to the transient nature of the complex, saturation effects can be observed on 
      the resonances of the unbound protein. The binding site comprises the hydrophobic 
      area surrounding the exposed copper ligand His81, suggesting that this residue is 
      important for efficient electron transfer.
FAU - Impagliazzo, Antonietta
AU  - Impagliazzo A
AD  - Leiden Institute of Chemistry, Leiden University, Gorlaeus Laboratories, PO Box 
      9502, 2300 RA Leiden, The Netherlands.
FAU - Ubbink, Marcellus
AU  - Ubbink M
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Am Chem Soc
JT  - Journal of the American Chemical Society
JID - 7503056
RN  - 0 (pseudoazurin)
RN  - 12284-43-4 (Azurin)
RN  - EC 1.7.- (Nitrite Reductases)
SB  - IM
MH  - Alcaligenes faecalis/enzymology
MH  - Azurin/*analogs & derivatives/*chemistry/*metabolism
MH  - Binding Sites
MH  - Models, Molecular
MH  - Molecular Weight
MH  - Nitrite Reductases/*chemistry/*metabolism
MH  - Nuclear Magnetic Resonance, Biomolecular
MH  - Protein Binding
MH  - Protein Conformation
EDAT- 2004/05/06 05:00
MHDA- 2004/07/29 05:00
CRDT- 2004/05/06 05:00
PHST- 2004/05/06 05:00 [pubmed]
PHST- 2004/07/29 05:00 [medline]
PHST- 2004/05/06 05:00 [entrez]
AID - 10.1021/ja049619h [doi]
PST - ppublish
SO  - J Am Chem Soc. 2004 May 12;126(18):5658-9. doi: 10.1021/ja049619h.