Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
8.3
5.5
Journals
Biomolecules
Special Issues
Advances in Heme Proteins
share announcement

Advances in Heme Proteins

A special issue of Biomolecules (ISSN 2218-273X).

Deadline for manuscript submissions: closed (31 October 2016) | Viewed by 5949

Special Issue Editor

Dr. Emily Weinert

E-Mail Website
Guest Editor
Department of Chemistry, Emory University, Atlanta, GA 30322, USA
Interests: heme sensors; bacterial oxygen sensing; cyclic nucleotide signaling

Special Issue Information

Dear Colleagues,

Heme proteins have evolved to conduct numerous functions, from catalysis to electron transfer to sensing. The explosion of available genome sequences has led to identification of heme proteins with novel catalytic activities and functions both in vitro and in vivo, and allowed for new insights into the role of the protein scaffold in controlling reactivity.

We encourage scientists investigating heme proteins using methods from diverse fields (biophysics, bioinorganic chemistry, enzymology, cell/micro-biology, etc.) to contribute a review or original research article exploring the structures and functions of heme proteins and model systems.

Dr. Emily Weinert
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Biomolecules is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • heme
  • P450
  • electron transfer
  • gas sensing
  • redox sensing
  • porphyrin chemistry
  • heme protein catalysis
  • porphyrin

Published Papers (1 paper)

Order results
Result details
Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:

Research

1964 KiB  
Article
Continuous Reusability using Immobilized HasApf in Chemoenzymatic Deracemization: A New Heterogeneous Enzyme Catalysis
by Hiroyuki Nagaoka
Biomolecules 2016, 6(4), 41; https://doi.org/10.3390/biom6040041 - 25 Oct 2016
Cited by 2 | Viewed by 5550
Abstract
This study found that the calibration curve of heme acquisition system A (HasA, a new reactive active species) immobilized by a porous ceramic particle (ImHApf; immobilized HasA from Pseudomonas fluorescens) can be constructed in the range of 1750–1450 cm−1 using Fourier [...] Read more.
This study found that the calibration curve of heme acquisition system A (HasA, a new reactive active species) immobilized by a porous ceramic particle (ImHApf; immobilized HasA from Pseudomonas fluorescens) can be constructed in the range of 1750–1450 cm−1 using Fourier transform infrared spectroscopy (FTIR) analysis, and evaluated its catalytic efficiency. In the asymmetric oxidation of rac-1-(6-methoxynaphthalen-2-yl)ethanol (rac-1: a naproxen precursor), a product ketone from the (R)-isomer is desymmetrized using NaBH4 and continuously reused even if treated with an organic solvent in 50 mM glycine–NaOH buffer at 40 °C in the absence of nicotinamide adenine dinucleotide (NAD(P)), leading to >99% enantiomeric excess and >90% chemical yield; the activity was calculated at 0.74 ± 0.03 mU/(mg·min) and the turnover number was determined to be approximately 2 × 106. It was confirmed that the other sec-alcohols such as rac-1-(2-naphthyl)ethanol (rac-2) and m- and p-substituted rac-1-phenyl ethanols (rac-3ab–6ab) using ImHApf can also yield a single stereoisomer from a racemate. Therefore, HasA immobilization can be expected to become an important tool for building an environmentally friendly system that promotes industrial sustainability. Full article
(This article belongs to the Special Issue Advances in Heme Proteins)
►▼ Show Figures

Graphical abstract

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-1
Back to TopTop