Microbial Hemoglobins

A special issue of Microorganisms (ISSN 2076-2607). This special issue belongs to the section "Molecular Microbiology and Immunology".

Deadline for manuscript submissions: closed (30 June 2021) | Viewed by 13708

Special Issue Editor


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Guest Editor
Illinois Institute of Technology, Chicago, IL, USA
Interests: molecular biology; microbiology; biochemistry; genetic engineering of bacteria; bacterial hemoglobin

Special Issue Information

Dear Colleagues,

The first bacterial hemoglobin was discovered in Vitreoscilla in 1986. Since that time, hemoglobins have been found in a wide range of bacteria (and archaebacteria). They can be grouped into several different structural classes and have a variety of functions. Beginning in 1990 and continuing today, engineering of heterologous hosts to express bacterial hemoglobins (especially that from Vitreoscilla) has been used to improve the production of valuable metabolites in microorganisms and even the growth and viability of higher plants.

The journal Microorganisms is planning a Special Issue on the topic of microbial hemoglobins and is soliciting contributions for this Special Issue. We encourage the submission of manuscripts (original research articles or reviews) on any aspect of microbial hemoglobins, including: their distribution among microbial species; their structural diversity (full-length, truncated, and two-domain flavohemoglobins); their biochemical functions; their effects on and connection to overall cell physiology; and their use (particularly through genetic engineering) to enhance the production of valuable metabolites in microorganisms and the growth and viability of higher plants.

Prof. Dr. Benjamin C. Stark
Guest Editor

Manuscript Submission Information

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Keywords

  • microbial hemoglobins
  • microbial productivity enhancement
  • flavohemoglobins
  • genetic engineering
  • oxygen sensing and metabolism
  • plant growth enhancement
  • truncated hemoglobins
  • Vitreoscilla hemoglobin

Published Papers (6 papers)

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Editorial

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1 pages, 142 KiB  
Editorial
Final Thoughts, Microorganisms Special Issue on Microbial Hemoglobins
by Benjamin C. Stark
Microorganisms 2022, 10(2), 379; https://doi.org/10.3390/microorganisms10020379 - 06 Feb 2022
Viewed by 816
Abstract
The year 2021 marked the thirty-fifth anniversary of the discovery of microbial hemoglobins by Dale Webster and his colleagues [...] Full article
(This article belongs to the Special Issue Microbial Hemoglobins)

Research

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15 pages, 3058 KiB  
Article
Translational Fusion to Hmp Improves Heterologous Protein Expression
by Xuanqing Wan, A. James Link and Mark P. Brynildsen
Microorganisms 2022, 10(2), 358; https://doi.org/10.3390/microorganisms10020358 - 04 Feb 2022
Cited by 1 | Viewed by 2003
Abstract
Flavohemoglobins, which are widely distributed in prokaryotes and eukaryotes, play key roles in oxygen (O2) transport and nitric oxide (·NO) defense. Hmp is the flavohemoglobin of Escherichia coli, and here we report that the translational fusion of Hmp to the [...] Read more.
Flavohemoglobins, which are widely distributed in prokaryotes and eukaryotes, play key roles in oxygen (O2) transport and nitric oxide (·NO) defense. Hmp is the flavohemoglobin of Escherichia coli, and here we report that the translational fusion of Hmp to the N-terminus of heterologous proteins increases their expression in E. coli. The effect required the fusion of the proteins, and was independent of both the O2-binding and catalytic activity of Hmp. Increased expression was at the translational level, likely to be downstream of initiation, and we observed that as little as the first 100 amino acids of Hmp were sufficient to boost protein production. These data demonstrate the potential of Hmp as an N-terminal fusion tag to increase protein yield, and suggest that the utility of bacterial hemoglobins to biotechnology goes beyond their O2 transport and ·NO detoxification capabilities. Full article
(This article belongs to the Special Issue Microbial Hemoglobins)
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10 pages, 1566 KiB  
Article
Effects of Efficient Expression of Vitreoscilla Hemoglobin on Production, Monosaccharide Composition, and Antioxidant Activity of Exopolysaccharides in Ganoderma lucidum
by Zi-Xu Wang, Na Li and Jun-Wei Xu
Microorganisms 2021, 9(8), 1551; https://doi.org/10.3390/microorganisms9081551 - 21 Jul 2021
Cited by 7 | Viewed by 1838
Abstract
A Vitreoscilla hemoglobin (VHb) gene was efficiently expressed by the optimization of codons and intron addition in G. lucidum. Expression of the VHb gene was confirmed by genome PCR, quantitative real-time PCR and carbon monoxide (CO)-difference spectrum analysis in the transformant. The [...] Read more.
A Vitreoscilla hemoglobin (VHb) gene was efficiently expressed by the optimization of codons and intron addition in G. lucidum. Expression of the VHb gene was confirmed by genome PCR, quantitative real-time PCR and carbon monoxide (CO)-difference spectrum analysis in the transformant. The effects of the efficient expression of VHb gene on production, monosaccharide compostion, and antioxidant activity of G. lucidum exopolysaccharides were studied. The maximum production of exopolysaccharides in the VHb gene-bearing transformant was 1.63 g/L, which was 1.5-fold higher than expression in the wild-type strain. Efficient expression of the VHb gene did not change the monosaccharide composition or distribution of molecular weight, but it increased the mole percentage ratio of galactose and mannose in G. lucidum exopolysaccharide. Exopolysaccharides from the transformant had higher scavenging 2,2-diphenyl-1-picrylhydrazyl (DPPH) and hydroxyl (OH) radical capacity and reducing power than those from the wild-type strain. These results may be helpful for increasing production and application of exopolysaccharides produced by G. lucidum fermentation. Full article
(This article belongs to the Special Issue Microbial Hemoglobins)
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Review

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12 pages, 1078 KiB  
Review
Vitreoscilla Haemoglobin: A Tool to Reduce Overflow Metabolism
by Hilal Taymaz-Nikerel and Alvaro R. Lara
Microorganisms 2022, 10(1), 43; https://doi.org/10.3390/microorganisms10010043 - 26 Dec 2021
Cited by 7 | Viewed by 2789
Abstract
Overflow metabolism is a phenomenon extended in nature, ranging from microbial to cancer cells. Accumulation of overflow metabolites pose a challenge for large-scale bioprocesses. Yet, the causes of overflow metabolism are not fully clarified. In this work, the underlying mechanisms, reasons and consequences [...] Read more.
Overflow metabolism is a phenomenon extended in nature, ranging from microbial to cancer cells. Accumulation of overflow metabolites pose a challenge for large-scale bioprocesses. Yet, the causes of overflow metabolism are not fully clarified. In this work, the underlying mechanisms, reasons and consequences of overflow metabolism in different organisms have been summarized. The reported effect of aerobic expression of Vitreoscilla haemoglobin (VHb) in different organisms are revised. The use of VHb to reduce overflow metabolism is proposed and studied through flux balance analysis in E. coli at a fixed maximum substrate and oxygen uptake rates. Simulations showed that the presence of VHb increases the growth rate, while decreasing acetate production, in line with the experimental measurements. Therefore, aerobic VHb expression is considered a potential tool to reduce overflow metabolism in cells. Full article
(This article belongs to the Special Issue Microbial Hemoglobins)
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8 pages, 460 KiB  
Review
The Discovery of Vitreoscilla Hemoglobin and Early Studies on Its Biochemical Functions, the Control of Its Expression, and Its Use in Practical Applications
by Dale A. Webster, Kanak L. Dikshit, Krishna R. Pagilla and Benjamin C. Stark
Microorganisms 2021, 9(8), 1637; https://doi.org/10.3390/microorganisms9081637 - 30 Jul 2021
Cited by 5 | Viewed by 1960
Abstract
In 1986, the surprising identification of a hemoglobin (VHb) in the bacterium Vitreoscilla greatly extended the range of taxa in which this oxygen binding protein functions. Elucidation of many of its biochemical properties and relation to overall cell physiology, as well as the [...] Read more.
In 1986, the surprising identification of a hemoglobin (VHb) in the bacterium Vitreoscilla greatly extended the range of taxa in which this oxygen binding protein functions. Elucidation of many of its biochemical properties and relation to overall cell physiology, as well as the sequence of the gene encoding it and aspects of control of its expression were determined in the following years. In addition, during the early years following its discovery, strategies were developed to use its expression in heterologous microbial hosts to enhance processes of practical usefulness. The VHb discovery also served as the foundation for what has become the fascinatingly rich field of bacterial hemoglobins. VHb’s position as the first known bacterial hemoglobin and its extensive use in biotechnological applications, which continue today, make a review of the early studies of its properties and uses an appropriate and interesting topic thirty-five years after its discovery. Full article
(This article belongs to the Special Issue Microbial Hemoglobins)
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13 pages, 1083 KiB  
Review
Recent Advances in the Physicochemical Properties and Biotechnological Application of Vitreoscilla Hemoglobin
by Fei Yu, Xinrui Zhao, Ziwei Wang, Luyao Liu, Lingfeng Yi, Jingwen Zhou, Jianghua Li, Jian Chen and Guocheng Du
Microorganisms 2021, 9(7), 1455; https://doi.org/10.3390/microorganisms9071455 - 07 Jul 2021
Cited by 12 | Viewed by 3504
Abstract
Vitreoscilla hemoglobin (VHb), the first discovered bacterial hemoglobin, is a soluble heme-binding protein with a faster rate of oxygen dissociation. Since it can enhance cell growth, product synthesis and stress tolerance, VHb has been widely applied in the field of metabolic engineering for [...] Read more.
Vitreoscilla hemoglobin (VHb), the first discovered bacterial hemoglobin, is a soluble heme-binding protein with a faster rate of oxygen dissociation. Since it can enhance cell growth, product synthesis and stress tolerance, VHb has been widely applied in the field of metabolic engineering for microorganisms, plants, and animals. Especially under oxygen-limited conditions, VHb can interact with terminal oxidase to deliver enough oxygen to achieve high-cell-density fermentation. In recent years, with the development of bioinformatics and synthetic biology, several novel physicochemical properties and metabolic regulatory effects of VHb have been discovered and numerous strategies have been utilized to enhance the expression level of VHb in various hosts, which greatly promotes its applications in biotechnology. Thus, in this review, the new information regarding structure, function and expressional tactics for VHb is summarized to understand its latest applications and pave a new way for the future improvement of biosynthesis for other products. Full article
(This article belongs to the Special Issue Microbial Hemoglobins)
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