Superoxide Dismutases

Patterson, David; Kunst, Catherine B.

doi:10.1002/0471203076.emm0468

Cited by 1 publication

(1 citation statement)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Superoxide dismutases [16][17][18] constitute the first line of cellular defense against oxidative stress arising from reactive oxygen species produced during aerobic respiration. [19][20][21][22] In order to protect the cells, these metalloenzymes catalyze the conversion of superoxide radicals (O2˙−) to produce hydrogen peroxide (H2O2) and molecular oxygen (O2) through alternate oxidation and reduction of their metal cofactor (M). 23 The overall dismutation reaction of superoxide is shown in equations (1) and (2) and the mechanism of SOD has been studied for several decades.…”

Section: Superoxide Dismutasesmentioning

confidence: 99%

Exploring the selectivity of metal ions in the active site of the enzyme superoxide dismutase (SOD) using site-directed mutagenesis

Rengifo¹

View full text Add to dashboard Cite

With love, to my parents (Genaro and Zenaida) and my brothers (Anibal, Samuel and Genaro) I would like to express my sincerest thanks and appreciation to my adviser, Professor Dr. Richard Garratt, for all his support, and vast knowledge on all things. Whenever I ran into trouble or had a question about the research, his office was always open. His observations and comments helped me to establish the overall direction of the research. I would like to specifically thank Prof. Dr. Jose Ribamar for the fruitful collaboration behind our mutational experiments, and for inspiring my creativity in research. I owe a debt of gratitude to Professor Dr. James Penner-Hahn for giving me the opportunity to work in his lab, for his absolute support of my thesis and for providing me with all the necessary facilities for our research collaboration. I am thankful to Prof. Dr. Pecoraro and Dr. Stuckey for the help and support during my stay in Michigan. I thank Dr. Annirudha and Postdoc Luis Basso for their assistance with the EPR experiments. I extend my gratitude also to Dr. Carol Ann Pitcairn for her care and precious friendship during my stay at the University of Michigan as well as her continued support and friendship thereafter.

show abstract

Section: Superoxide Dismutasesmentioning

confidence: 99%

Exploring the selectivity of metal ions in the active site of the enzyme superoxide dismutase (SOD) using site-directed mutagenesis

Rengifo¹

View full text Add to dashboard Cite

show abstract

Superoxide Dismutases

Cited by 1 publication

References 23 publications

Exploring the selectivity of metal ions in the active site of the enzyme superoxide dismutase (SOD) using site-directed mutagenesis

Exploring the selectivity of metal ions in the active site of the enzyme superoxide dismutase (SOD) using site-directed mutagenesis

Contact Info

Product

Resources

About