Spectroscopic characterization of a truncated hemoglobin from the nitrogen-fixing bacterium Herbaspirillum seropedicae
G Razzera, J Vernal, D Baruh, VI Serpa… - JBIC Journal of …, 2008 - Springer
The Herbaspirillum seropedicae genome sequence encodes a truncated hemoglobin typical
of group II (Hs-trHb1) members of this family. We show that His-tagged recombinant Hs …
of group II (Hs-trHb1) members of this family. We show that His-tagged recombinant Hs …
Chimeric β-EF3-α hemoglobin (Ψ): Energetics of subunit interaction and ligand binding
L Kiger, A Dumoulin, SJ Edelstein, DJ Abraham… - Biochemistry, 1998 - ACS Publications
Among the numerous strategies to design an oxygen carrier, we outline in this work the
engineering of a stable homotetrameric hemoglobin, expressed in Escherichia coli. The …
engineering of a stable homotetrameric hemoglobin, expressed in Escherichia coli. The …
The diversity of 2/2 (truncated) globins
Small size globins that have been defined as 'truncated haemoglobins' or as '2/2
haemoglobins' have increasingly been discovered in microorganisms since the early 1990s …
haemoglobins' have increasingly been discovered in microorganisms since the early 1990s …
Mechanism of the Nitric Oxide Dioxygenase Reaction of Mycobacterium tuberculosis Hemoglobin N
LA Carabet, M Guertin, P Lague… - The Journal of Physical …, 2017 - ACS Publications
Many globins convert• NO to innocuous NO3–through their nitric oxide dioxygenase (NOD)
activity. Mycobacterium tuberculosis fights the oxidative and nitrosative stress imposed by its …
activity. Mycobacterium tuberculosis fights the oxidative and nitrosative stress imposed by its …
Evaluating cooperativity in dimeric hemoglobins
A Boffi, E Chiancone - Methods in enzymology, 2004 - Elsevier
Publisher Summary A growing number of homo-and heterodimeric hemoglobins have been
identified not only within several phyla of invertebrates and lower vertebrates, but also in …
identified not only within several phyla of invertebrates and lower vertebrates, but also in …
Mechanistic insight into the enzymatic reduction of truncated hemoglobin N of Mycobacterium tuberculosis: role of the CD loop and pre-A motif in electron cycling
Many pathogenic microorganisms have evolved hemoglobin-mediated nitric oxide (NO)
detoxification mechanisms, where a globin domain in conjunction with a partner reductase …
detoxification mechanisms, where a globin domain in conjunction with a partner reductase …
The truncated oxygen-avid hemoglobin from Bacillus subtilis: X-ray structure and ligand binding properties
The group II truncated hemoglobin from Bacillus subtilis has been cloned, expressed,
purified, and characterized. B. subtilis truncated hemoglobin is a monomeric protein …
purified, and characterized. B. subtilis truncated hemoglobin is a monomeric protein …
Hemoglobin, an “evergreen” red protein
After more than a century of experimental, theoretical and computational studies, there is no
general agreement yet on the mechanisms underlying the fine regulation of hemoglobin …
general agreement yet on the mechanisms underlying the fine regulation of hemoglobin …
Dehaloperoxidase: An enzymatic Swiss army knife
T Malewschik, RA Ghiladi - Coordination Chemistry Reviews, 2021 - Elsevier
The hemoglobin from the marine worm Amphitrite ornata has been found to possess
multiple enzymatic activities in addition to its O 2-transport function. Named …
multiple enzymatic activities in addition to its O 2-transport function. Named …
Functional consequences of the creation of an Asp-His-Fe triad in a 3/3 globin
EL D'Antonio, J D'Antonio, V de Serrano, H Gracz… - Biochemistry, 2011 - ACS Publications
The proximal side of dehaloperoxidase-hemoglobin A (DHP A) from Amphitrite ornata has
been modified via site-directed mutagenesis of methionine 86 into aspartate (M86D) to …
been modified via site-directed mutagenesis of methionine 86 into aspartate (M86D) to …