Molecular aspects of bacterial nanocellulose biosynthesis

P Jacek, F Dourado, M Gama… - Microbial …, 2019 - Wiley Online Library
Bacterial nanocellulose (BNC) produced by aerobic bacteria is a biopolymer with
sophisticated technical properties. Although the potential for economically relevant …

Bacterial hemoglobins and flavohemoglobins: versatile proteins and their impact on microbiology and biotechnology

AD Frey, PT Kallio - FEMS microbiology reviews, 2003 - academic.oup.com
In response to oxygen limitation or oxidative and nitrosative stress, bacteria express three
kinds of hemoglobin proteins: truncated hemoglobins (tr Hbs), hemoglobins (Hbs) and …

Use of genetically engineered microorganisms (GEMs) for the bioremediation of contaminants

M Urgun-Demirtas, B Stark, K Pagilla - Critical reviews in …, 2006 - Taylor & Francis
This paper presents a critical review of the literature on the application of genetically
engineered microorganisms (GEMs) in bioremediation. The important aspects of using …

Enhanced bacterial cellulose production by Gluconacetobacter xylinus via expression of Vitreoscilla hemoglobin and oxygen tension regulation

M Liu, S Li, Y Xie, S Jia, Y Hou, Y Zou… - Applied microbiology and …, 2018 - Springer
Oxygen plays a key role during bacterial cellulose (BC) biosynthesis by Gluconacetobacter
xylinus. In this study, the Vitreoscilla hemoglobin (VHb)-encoding gene vgb, which has been …

Recent applications of Vitreoscilla hemoglobin technology in bioproduct synthesis and bioremediation

BC Stark, KR Pagilla, KL Dikshit - Applied microbiology and biotechnology, 2015 - Springer
Since its first use in 1990 to enhance production of α-amylase in E. coli, engineering of
heterologous hosts to express the hemoglobin from the bacterium Vitreoscilla (VHb) has …

High-efficiency expression of alginate lyase in Pichia pastoris facilitated by Vitreoscilla hemoglobin

Z Gu, F Niu, Z Yu, Z Bao, H Mukhtar, P Yang… - International Journal of …, 2024 - Elsevier
Vitreoscilla hemoglobin (VHb) can enhance the ability of recombinant strains to express
heterologous proteins under low-oxygen conditions. However, its mechanism of action in the …

Flavohemoglobin: structure and reactivity

A Bonamore, A Boffi - IUBMB life, 2008 - Wiley Online Library
Flavohemoglobins (flavoHbs) are made of a globin domain fused with a ferredoxin
reductaselike FAD‐and NAD‐binding modules. These proteins are widely represented …

The X-ray Structure of Ferric Escherichia coliFlavohemoglobin Reveals an Unexpected Geometry of the Distal Heme Pocket

A Ilari, A Bonamore, A Farina, KA Johnson… - Journal of Biological …, 2002 - ASBMB
The x-ray structure of ferric unliganded lipid-free Escherichia coli flavohemoglobin has been
solved to a resolution of 2.2 Å and refined to anR-factor of 19%. The overall fold is similar to …

Vitreoscilla hemoglobin binds to subunit I of cytochrome bo ubiquinol oxidases

KW Park, KJ Kim, AJ Howard, BC Stark… - Journal of Biological …, 2002 - ASBMB
The bacterium, Vitreoscilla, can induce the synthesis of a homodimeric hemoglobin under
hypoxic conditions. Expression of VHb in heterologous bacteria often enhances growth and …

Hemoglobin: a nitric‐oxide dioxygenase

PR Gardner - Scientifica, 2012 - Wiley Online Library
Members of the hemoglobin superfamily efficiently catalyze nitric‐oxide dioxygenation, and
when paired with native electron donors, function as NO dioxygenases (NODs). Indeed, the …