Myoglobin electrochemistry

G.C. Zhao, L. Zhang, X.W. Wei, Z.S. Yang, Myoglobin on multi-walled carbon nanotubes modified electrode direct electrochemistry and electrocatalysis. Electrochem. Commun. 5, 825—829 (2003). 

Y.D. Jin, Y. Shao, and S.J. Dong, Direct electrochemistry and surface plasmon resonance characterization of alternate layer-by-layer self-assembled DNA-myoglobin thin films on chemically modified gold surfaces. Langmuir 19, 4771—4777 (2003). 

Y.J. Hu, N.F. Hu, and Y.H. Zeng, Electrochemistry and electrocatalysis with myoglobin in biomembrane-like surfactant-polymer 2C 2N+PA composite films. Talanta 50, 1183-1195 (2000). 

L.W. Wang and N.F Hu, Electrochemistry and electrocatalysis with myoglobin in biomembrane-like DHP-PDDA polyelectrolyte-surfactant complex films. J. Colloid Interface Sci. 236, 166—172 (2001). 

N.F. Hu and J.F. Rusling, Electrochemistry and catalysis with myoglobin in hydrated poly(ester sulfonic acid) ionomer films. Langmuir 13, 4119-4125 (1997). 

L. Shen, R. Huang, and N.F. Hu, Myoglobin in polyacrylamide hydrogel films direct electrochemistry and electrochemical catalysis. Talanta 56, 1131-1139 (2002). 

The first electrochemical studies of Mb were reported for the horse heart protein in 1942 (94) and subsequently for sperm whale Mb (e.g., 95) through use of potentiometric titrations employing a mediator to achieve efficient equilibriation of the protein with the electrode (96). More recently, spectroelectrochemical measurements have also been employed (97, 98). The alternative methods of direct electrochemistry (99-102) that are used widely for other heme proteins (e.g., cytochrome c, cytochrome bs) have not been as readily applied to the study of myoglobin because coupling the oxidation-reduction eqiulibrium of this protein to a modified working electrode surface has been more difficult to achieve. As a result, most published electrochemical studies of wild-type and variant myoglobins have involved measurements at eqiulibrium rather than dynamic techniques. 

Recent work has resolved some of the issues that complicate direct electrochemistry of myoglobin, and, in fact, it has been demonstrated that Mb can interact effectively with a suitable electrode surface (103-113). This achievement has permitted the investigation of more complex aspects of Mb oxidation-reduction behavior (e.g., 106). In general, it appears that the primary difficulty in performing direct electrochemistry of myoglobin results from the change in coordination number that accompanies conversion of metMb (six-coordinate) to reduced (deoxy) Mb (five-coordinate) and the concomitant dissociation of the water molecule (or hydroxide at alkaline pH) that provides the distal ligand to the heme iron of metMb. 

Wright, M., Honeychurch, M.J., Hill, H. and Allen O. (1999) Bioelectrochemical dehalogenations via direct electrochemistry of poly(ethylene oxide)-modified myoglobin. Electrochem. Com-mun. 1,609-613. 

Microperoxidase-11, MP-11, is a heme-undecapeptide that is prepared by the digestion of cytochrome c and it includes the active surrounding of cytochrome MP-11 was immobilized on electrode surface s and its electrochemistry was characterized. The MP-11-modified electrodes were reported to act as effective electron mediator interfaces for the reduction of cytochrome c, hemoglobin, myoglobin and nitrate reductase (cytochrome c-dependent). The MP-11-mediated activation of nitrate reductase, NR, was employed to assemble an integrated MP-11/NR electrode for the bioelectrocatalyzed reduction of nitrate (NO3 ) to nitrite (NO2). An affinity complex between a MP-11-functionalized electrode and NR (/Q = 3.7x10 M ) was crosslinked with glutaric dialdehyde to yield the electrically contacted electrode for the bioelectrocatalyzed reduction of nitrate to nitrite. In this system the reduced MP-11 mediates ET to NR and activates the enzyme towards the reduction of NO3. 

Soc., 1999, 121, 3435 T. Hoshi, H. Saiki, S. Kuwazawa, Y. Kobayama and A. Anzai, Polyelectrolyte multilayer film-coated electrodes for amperometric determination of hydrogen peroxide in the presence of ascorbic acid, uric acid and acetaminophen, Anal. Sci., 2000, 16, 1009 E.S. Forzani, VM. Solis and E.J. Calvo, Electrochemical behavior of polyphenol oxidase immobilized in self-assembled structures layer by layer with cationic polyallylamine, Anal. Chem., 2000, 72, 5300 Y.M. Lvov, Z. Lu, J.B. Schenkman, X. Zu and J.F. Rusling, Direct electrochemistry of myoglobin and cytochrome P450cam in alternate layer-by-layer film with DNA and other polyions, J. Am. Chem. Soc., 1998, 120, 4073. 

Y.M. Lvov, Z.Q. Lu, J.B. Schenkman, and J.R Rusling, Direct electrochemistry of myoglobin and cytochrome P450cam in alternate polyion layer-by-layer films. J. Am. Chem. Soc. 120, 4073-4080 (1998). 

---