Ammonia‐oxidizing bacteria: their biochemistry and molecular biology
LA Sayavedra‐Soto, DJ Arp - Nitrification, 2011 - Wiley Online Library
This chapter covers the current understanding of the biochemical and genetic underpinnings
relevant to ammonia oxidation by aerobic bacteria. Ammonia is released into the …
relevant to ammonia oxidation by aerobic bacteria. Ammonia is released into the …
NO Reductase Activity of the Tetraheme Cytochrome c554 of Nitrosomonas europaea
AK Upadhyay, AB Hooper… - Journal of the American …, 2006 - ACS Publications
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 …
function as an electron-transfer protein from hydroxylamine oxidoreductase (HAO). We show …
Dicyandiamide addition delay nitrous oxide emission and shift its production pathway from denitrification to incomplete nitrification in maturation phase of composting
Y Liu, R Tang, G Liu, G Li, J Wang, Y Cai… - Chemical Engineering …, 2024 - Elsevier
Nitrous oxide (N 2 O) emissions contribute to nitrogen loss and exacerbate the greenhouse
effect during composting. Investigating the efficacy and underlying mechanisms of …
effect during composting. Investigating the efficacy and underlying mechanisms of …
Genomics of ammonia‐oxidizing bacteria and insights into their evolution
This chapter talks about ammonium‐oxidizing bacteria (AOB), addresses the inventory
involved in nitrification, attempts metabolic reconstruction of N transformation processes …
involved in nitrification, attempts metabolic reconstruction of N transformation processes …
Kinetic and product distribution analysis of NO· reductase activity in Nitrosomonas europaea hydroxylamine oxidoreductase
J Kostera, MD Youngblut, JM Slosarczyk… - JBIC Journal of …, 2008 - Springer
Hydroxylamine oxidoreductase (HAO) from the ammonia-oxidizing bacterium Nitrosomonas
europaea normally catalyzes the four-electron oxidation of hydroxylamine to nitrite, which is …
europaea normally catalyzes the four-electron oxidation of hydroxylamine to nitrite, which is …
[HTML][HTML] Cytochromes P460 and c′-beta; a new family of high-spin cytochromes c
BO Elmore, DJ Bergmann, MG Klotz, AB Hooper - FEBS letters, 2007 - Elsevier
Cytochromes-P460 of Nitrosomonas europaea and Methylococcus capsulatus (Bath), and
the cytochrome c′ of M. capsulatus, believed to be involved in binding or transformation of …
the cytochrome c′ of M. capsulatus, believed to be involved in binding or transformation of …
Do multiheme cytochromes containing close-packed heme groups have a band structure formed from the heme π and π* orbitals?
JH van Wonderen, A Morales-Florez, TA Clarke… - Current Opinion in …, 2024 - Elsevier
Multiheme cytochromes (MHCs) are bacterial electron-transfer proteins. We show from
optical spectra and calculations that some of these cytochromes probably contain occupied …
optical spectra and calculations that some of these cytochromes probably contain occupied …
Heme and hemoproteins
Heme cofactors are found in a wide range of proteins, where they play various roles in eg,
steroid and bioactive lipid synthesis, energy transduction, gene regulation,'cellular signaling …
steroid and bioactive lipid synthesis, energy transduction, gene regulation,'cellular signaling …
Structural and Biochemical Characterization of DHC2, a Novel Diheme Cytochrome c from Geobacter sulfurreducens,
D Heitmann, O Einsle - Biochemistry, 2005 - ACS Publications
Multiheme cytochromes c constitute a widespread class of proteins with essential functions
in electron transfer and enzymatic catalysis. Their functional properties are in part …
in electron transfer and enzymatic catalysis. Their functional properties are in part …
The 1.25 Å Resolution Structure of the Diheme NapB Subunit of Soluble Nitrate Reductase Reveals a Novel Cytochrome c Fold with a Stacked Heme Arrangement,
A Brigé, D Leys, TE Meyer, MA Cusanovich… - Biochemistry, 2002 - ACS Publications
The diheme cytochrome NapB constitutes the small subunit of a periplasmic nitrate
reductase found in a wide variety of bacterial species, including pathogens. The NapB …
reductase found in a wide variety of bacterial species, including pathogens. The NapB …