The cytochrome cd1 nitrite reductases are enzymes that catalyse the reduction of nitrite to nitric oxide (NO) in the bacterial energy conversion denitrification process. These enzymes contain two different redox centres: one covalently bound c-haem, which is reduced by external donors, and one peculiar d1-haem, where catalysis occurs. In the present paper, we summarize the current understanding of the reaction of nitrite reduction in the light of the most recent results on the enzyme from Pseudomonas aeruginosa and discuss the differences between enzymes from different organisms. We have evidence that release of NO from the ferrous d1-haem occurs rapidly enough to be fully compatible with the turnover, in contrast with previous hypotheses, and that the substrate nitrite is able to displace NO from the d1-haem iron. These results shed light on the mechanistic details of the activity of cd1 nitrite reductases and on the biological role of the d1-haem, whose presence in this class of enzymes has to date been unexplained.
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December 2008
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Conference Article|
November 19 2008
New insights into the activity of Pseudomonas aeruginosa cd1 nitrite reductase
Serena Rinaldo;
Serena Rinaldo
*Dipartimento di Scienze Biochimiche “A. Rossi Fanelli” and Istituto di Biologia e Patologia Molecolari del CNR
†Istituto di Biochimica e Biochimica Clinica, Università Cattolica del Sacro Cuore, Rome, Italy
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Alessandro Arcovito;
Alessandro Arcovito
†Sapienza, Università di Roma, Rome, Italy
†Istituto di Biochimica e Biochimica Clinica, Università Cattolica del Sacro Cuore, Rome, Italy
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Giorgio Giardina;
Giorgio Giardina
*Dipartimento di Scienze Biochimiche “A. Rossi Fanelli” and Istituto di Biologia e Patologia Molecolari del CNR
†Istituto di Biochimica e Biochimica Clinica, Università Cattolica del Sacro Cuore, Rome, Italy
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Nicoletta Castiglione;
Nicoletta Castiglione
*Dipartimento di Scienze Biochimiche “A. Rossi Fanelli” and Istituto di Biologia e Patologia Molecolari del CNR
†Istituto di Biochimica e Biochimica Clinica, Università Cattolica del Sacro Cuore, Rome, Italy
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Maurizio Brunori;
Maurizio Brunori
*Dipartimento di Scienze Biochimiche “A. Rossi Fanelli” and Istituto di Biologia e Patologia Molecolari del CNR
†Istituto di Biochimica e Biochimica Clinica, Università Cattolica del Sacro Cuore, Rome, Italy
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Francesca Cutruzzolà
Francesca Cutruzzolà
1
*Dipartimento di Scienze Biochimiche “A. Rossi Fanelli” and Istituto di Biologia e Patologia Molecolari del CNR
†Istituto di Biochimica e Biochimica Clinica, Università Cattolica del Sacro Cuore, Rome, Italy
1To whom correspondence should be addressed (email francesca.cutruzzola@uniroma1.it).
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Publisher: Portland Press Ltd
Received:
June 04 2008
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2008 Biochemical Society
2008
Biochem Soc Trans (2008) 36 (6): 1155–1159.
Article history
Received:
June 04 2008
Citation
Serena Rinaldo, Alessandro Arcovito, Giorgio Giardina, Nicoletta Castiglione, Maurizio Brunori, Francesca Cutruzzolà; New insights into the activity of Pseudomonas aeruginosa cd1 nitrite reductase. Biochem Soc Trans 1 December 2008; 36 (6): 1155–1159. doi: https://doi.org/10.1042/BST0361155
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