Multi-haem cytochromes are employed by a range of microorganisms to transport electrons
over distances of up to tens of nanometres. Perhaps the most spectacular utilization of these …

The metallobiochemistry underlying the formation of the inorganic N–N-bond-containing
molecules nitrous oxide (N2O), dinitrogen (N2), and hydrazine (N2H4) is essential to the …

CymA (tetrahaem cytochrome c) is a member of the NapC/NirT family of quinol
dehydrogenases. Essential for the anaerobic respiratory flexibility of shewanellae, CymA …

While iron is often a limiting nutrient to Biology, when the element is found in the form of
heme cofactors (iron protoporphyrin IX), living systems have excelled at modifying and …

Anaerobic ammonium-oxidizing (anammox) bacteria convert nitrite and ammonium via nitric
oxide (NO) and hydrazine into dinitrogen gas by using a diverse array of proteins, including …

Heme is one of the most pervasive cofactors in nature and the c-type cytochromes represent
one of the largest families of heme-containing proteins. Recent progress in bacterial …

This chapter covers the current understanding of the biochemical and genetic underpinnings
relevant to ammonia oxidation by aerobic bacteria. Ammonia is released into the …

The tetraheme cytochrome c 554 (cyt c 554) from Nitrosomonas europaea is believed to
function as an electron-transfer protein from hydroxylamine oxidoreductase (HAO). We show …

MauG is a novel 42 kDa diheme protein which is required for the biosynthesis of tryptophan
tryptophylquinone, the prosthetic group of methylamine dehydrogenase. The visible …

Hydroxylamine oxidoreductase (HAO) from the ammonia-oxidizing bacterium Nitrosomonas
europaea normally catalyzes the four-electron oxidation of hydroxylamine to nitrite, which is …