@article {2501,
	title = {Electrochemical studies on nitrite reductase towards a biosensor},
	journal = {Biochem Biophys Res Commun},
	volume = {209},
	number = {3},
	year = {1995},
	note = {<p>0006-291X (Print)0006-291X (Linking)Journal ArticleResearch Support, Non-U.S. Gov{\textquoteright}tResearch Support, U.S. Gov{\textquoteright}t, Non-P.H.S.</p>
},
	month = {Apr 26},
	pages = {1018-25},
	abstract = {<p>A c-type hexaheme nitrite reductase (NiR) isolated from nitrate-grown cells of Desulfovibrio desulfuricans (Dd) ATCC 27774 catalyses the six-electron reduction of nitrite to ammonia. Previous electrochemical studies demonstrated that a simple electrocatalytic mechanism can be applied to this system (Moreno, C., Costa, C., Moura, I., LeGall, J., Liu, M. Y., Payne, W. J., Van Dijk, C. and Moura, J. J. G. (1992) Eur.J.Biochem. 212, 79-86). Its substrate specificity, availability and stability under ambient conditions makes this enzymatic system a promising candidate for use in a biosensor device. An electrochemical study of gel-immobilized Dd NiR on a glassy carbon electrode revealed both enzymatic activity and amperometric response to nitrite. In this study it was observed that the catalytic current density is a function of the nitrite concentration in solution and follows a characteristic Michaelis-Menten-type substrate dependence. Such a biosensor device (NiR-electrode) bears the option to be used for analytical determination of nitrite in complex media.</p>
},
	keywords = {Biosensing Techniques, Desulfovibrio/*enzymology/growth \& development, Electrochemistry/methods, Enzymes, Immobilized/analysis/*metabolism, Kinetics, Nitrite Reductases/analysis/*metabolism, Oxidation-Reduction, Potentiometry/methods},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list_uids=7733953 },
	author = {Scharf, M. and Moreno, C. and Costa, C. and Van Dijk, C. and Payne, W. J. and Legall, J. and Moura, I. and Moura, J. J.}
}
