Ascorbate Protects the Di-Heme Enzyme, MauG, Against Self-Inflicted Oxidative Damage by an Unusual Antioxidant Mechanism

Por Ma, Zhongxin, Davidson, Victor L.
Publicado no Biochem J (2017)

Redox properties of a cysteine tryptophylquinone-dependent glycine oxidase are distinct from those of tryptophylquinone-dependent dehydrogenases

Por Ma, Zhongxin, Davidson, Victor L.
Publicado no Biochemistry (2019)

Roles of multiple-proton transfer pathways and proton-coupled electron transfer in the reactivity of the bis-Fe(IV) state of MauG

Por Ma, Zhongxin, Williamson, Heather R., Davidson, Victor L.
Publicado no Proc Natl Acad Sci U S A (2015)

Mechanism of protein oxidative damage that is coupled to long-range electron transfer to high-valent hemes

Por Ma, Zhongxin, Williamson, Heather R., Davidson, Victor L.
Publicado no Biochem J (2016)

A suicide mutation affecting proton transfers to high-valent hemes causes inactivation of MauG during catalysis

Por Ma, Zhongxin, Williamson, Heather R., Davidson, Victor L.
Publicado no Biochemistry (2016)

Properties of the high-spin heme of MauG are altered by binding of preMADH at the protein surface 40 Å away

Por Feng, Manliang, Ma, Zhongxin, Crudup, Breland F., Davidson, Victor L.
Publicado no FEBS Lett (2017)

The Rv2633c protein of Mycobacterium tuberculosis is a non-heme di-iron catalase with a possible role in defenses against oxidative stress

Por Ma, Zhongxin, Strickland, Kyle T., Cherne, Michelle D., Sehanobish, Esha, Rohde, Kyle H., Self, William T., Davidson, Victor L.
Publicado no J Biol Chem (2018)