Article
Microbiology
Sirui Han, Kailun Guo, Wei Wang, Yizhi J. Tao, Haichun Gao
Summary: In this study, HtpA was identified as a heme-trafficking protein in the bacterium Shewanella oneidensis. The absence of HtpA significantly reduced cytochrome c content and catalase activity. This research sheds light on the mechanism of heme transport across membranes in bacteria and extends the understanding of TANGO2 proteins.
Article
Chemistry, Analytical
Mehmet Yunus Genceroglu, Cansu Cavdar, Selen Manioglu, Halil Bayraktar
Summary: This study presents a genetically encoded fluorescence method for monitoring the conformational changes of Cytc upon binding to heme and CCHL. The results show that the noncovalent interaction of heme in the absence of CCHL induces a partially folded state of Cytc, while higher concentrations of heme and coexpression of CCHL lead to the recovery of Cytc native structure.
Article
Multidisciplinary Sciences
Luke E. Formosa, Shadi Maghool, Alice J. Sharpe, Boris Reljic, Linden Muellner-Wong, David A. Stroud, Michael T. Ryan, Megan J. Maher
Summary: COA7 is a crucial assembly factor for the biogenesis of mitochondrial complex IV. It interacts with SCO1 and SCO2 to catalyze copper relay and reduction of disulfide bonds, which are important for complex IV assembly.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
(2022)
Article
Crystallography
Rita Chertkova, Tatyana Bryantseva, Nadezhda A. Brazhe, Kseniya S. Kudryashova, Victor V. Revin, Alexei N. Nekrasov, Alexander Yusipovich, Alexey R. Brazhe, Andrew B. Rubin, Dmitry A. Dolgikh, Mikhail P. Kirpichnikov, Georgy Maksimov
Summary: The secondary structure of horse cytochrome c with mutations in the P(76)GTKMIFA(83) site of the Omega-loop, exhibiting reduced efficiency of electron transfer, was studied. CD spectroscopy and IR spectroscopy data showed changes in structural elements, with an increase in beta-structural elements and a decrease in non-structured elements. H-1-NMR spectra analysis revealed specific features in the secondary structure related to changes in the heme microenvironment. These changes likely contribute to the decreased efficiency of electron transfer in the studied cytochromes c.
Article
Biochemistry & Molecular Biology
Srijeeb Karmakar, Arjun Sankhla, Vimal Katiyar
Summary: The holo form of Cytochrome-C remains structurally intact in the presence of heme, but prolonged thermal and pH stress can lead to dissociation of heme, resulting in the collapse of the protein structure into a macromolecular amyloid-network and FeQDs with 2-3 nm diameter. Further studies revealed that FeQDs can re-adsorb on the surface of the amyloid network, forming a FeQD-decorated amyloid matrix. Excitingly, the FeQDs exhibit gel-like properties and support cell growth without cytotoxicity, suggesting potential for diverse biological applications as advanced biomaterials.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2021)
Article
Microbiology
Amber L. Grunow, Susan C. Carroll, Alicia N. Kreiman, Molly C. Sutherland
Summary: Heme trafficking is a fundamental biological process, and studying it has been challenging due to its tight regulation, cytotoxicity, and transient nature. The bacterial cytochrome c biogenesis pathways, especially System I, provide a model for understanding heme trafficking mechanisms. A detailed analysis of the WWD domain in CcmF reveals its interaction with heme and its role in attaching heme to apocytochrome c. This analysis also uncovers common mechanisms of heme interaction in different heme trafficking pathways.
Article
Engineering, Environmental
Chia-Lun Ho, Mohammed Y. Emran, Souta Ihara, Wenyuan Huang, Satoshi Wakai, Wei-Peng Li, Akihiro Okamoto
Summary: Labeling electrogenic bacteria from a microbiota was achieved by polymerizing 3,3'-diaminobenzidine (DAB) monomers to form DAB polymer and depositing it on the cell surface. The labeled electrogenic bacteria were then enriched through specific conjugation with magnetic nanoparticle surfaces. This rapid enrichment strategy has the potential to improve the efficiency of microbial electrochemical technologies and facilitate the identification of electrogenic bacteria.
CHEMICAL ENGINEERING JOURNAL
(2023)
Article
Biotechnology & Applied Microbiology
Wei Wang, Yawen Liang, Lulu Liu, Sirui Han, Shihua Wu, Haichun Gao
Summary: In S. oneidensis, Hfq plays a critical role in regulating the content of cytochromes c and pyomelanin production by differentially regulating heme biosynthesis and degradation, as well as HmgA activity through modulating intracellular iron levels.
APPLIED AND ENVIRONMENTAL MICROBIOLOGY
(2022)
Article
Agriculture, Multidisciplinary
Jian Wu, Qingzhu Teng, Yushuai Mao, Yabing Duan, Xiayan Pan, Shu Xu, Yiqiang Cai, Yuemin Pan, Mingguo Zhou, Yong Zhang
Summary: The study found that the cytochrome bc1 complex plays a critical and conserved role in tolerating phenazines in Xanthomonas, and that cytochrome C4 is key in revealing the tolerance mechanism. This research provides a potential strategy to improve the activity of phenazines against Xanthomonas.
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
(2022)
Review
Biochemistry & Molecular Biology
Elise D. Rivett, Lim Heo, Michael Feig, Eric L. Hegg
Summary: The passage discusses the key step of heme synthesis in aerobic respiration, focusing on the newly gained insights from structural studies on heme o synthase (HOS) and heme a synthase (HAS). It highlights the proposed catalytic mechanisms and the implications of the new structural data for understanding heme trafficking and heme-copper oxidase assembly in the broader context of the heme a biosynthetic pathway.
CRITICAL REVIEWS IN BIOCHEMISTRY AND MOLECULAR BIOLOGY
(2021)
Article
Chemistry, Multidisciplinary
H. Christopher Fry, Ralu Divan, Yuzi Liu
Summary: The design of peptide amphiphiles that assemble into 1D nanostructures and yield metalloporphyrin binding sites is presented. By exploring different peptide assemblies, it is found that the sequence with a length of 2 has the highest binding affinity. These nanoscale assemblies have ordered arrays of heme and show potential utility in sensing and enzymatic materials.
Article
Engineering, Environmental
Xizi Long, Yoshihide Tokunou, Akihiro Okamoto
Summary: Bacterial outer-membrane multi-heme cytochromes (OMCs) can modify heme coupling through mechanical interactions among OMCs by controlling their concentrations. The concentration of OMCs significantly impacts their circular dichroism (CD) spectra and redox property, resulting in a 4-fold change in microbial current production. Overexpression of OMCs increases the conductive current across the biofilm, indicating enhanced inter-protein electron hopping via collision on the cell surface.
ENVIRONMENTAL SCIENCE & TECHNOLOGY
(2023)
Article
Biochemistry & Molecular Biology
Elise D. Rivett, Hannah G. Addis, Jonathan V. Dietz, Jayda A. Carroll-Deaton, Shipra Gupta, Koji L. Foreman, Minh Anh Dang, Jennifer L. Fox, Oleh Khalimonchuk, Eric L. Hegg
Summary: In aerobic respiration, heme a is required for the final step catalyzed by aa3-type cytochrome c oxidase. The conversion of heme b to heme o and ultimately to heme a is achieved through two modifications, with the conversion of a methyl group to an aldehyde being catalyzed by heme a synthase (HAS). Previous studies have shown that HAS contains two heme-binding sites, with one site occupied by heme b. However, the function of the other site is still unknown.
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
(2023)
Article
Biochemistry & Molecular Biology
Nadezda A. Brazhe, Evelina I. Nikelshparg, Adil A. Baizhumanov, Vera G. Grivennikova, Anna A. Semenova, Sergey M. Novikov, Valentyn S. Volkov, Aleksey V. Arsenin, Dmitry I. Yakubovsky, Andrey B. Evlyukhin, Zhanna V. Bochkova, Eugene A. Goodilin, Georgy V. Maksimov, Olga Sosnovtseva, Andrey B. Rubin
Summary: A novel sensor using label-free surface-enhanced Raman spectroscopy (SERS) has been developed to identify conformational changes in cytochrome c heme and elucidate its role in functioning mitochondria. It has been shown that molecule bond vibrations assessed by SERS are a reliable indicator of heme conformation, which regulates the efficiency of the mitochondrial respiratory chain and adjusts mitochondrial respiration to the cell's consumption of ATP.
FREE RADICAL BIOLOGY AND MEDICINE
(2023)
Review
Biochemistry & Molecular Biology
Marina A. Semenova, Rita V. Chertkova, Mikhail P. Kirpichnikov, Dmitry A. Dolgikh
Summary: Neuroglobin, a heme protein predominantly expressed in nervous tissue, has been shown to promote neuronal survival. However, the molecular mechanisms underlying its neuroprotective function remain unclear. Recent experimental and computational work suggests that the interaction between neuroglobin and mitochondrial cytochrome c may contribute to neuroglobin-mediated neuroprotection, both in the cytoplasm and within the mitochondria.