Article
Chemistry, Multidisciplinary
Qinzhen Li, Baoyu Huang, Sha Yang, Hui Zhang, Jinsong Chai, Yong Pei, Manzhou Zhu
Summary: This study provides a deep insight into the origin and structural transition of gold nanoclusters from organometallic complexes. The research reveals that the evolution from organometallic complexes to nanoclusters is accompanied by a significant decrease in HOMO-LUMO gaps, and the formation of the first Au-Au bond is captured in the Au-13 nanocluster.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2021)
Article
Biochemistry & Molecular Biology
Xi Liu, Laixing Zhang, Yu Xiu, Teng Gao, Ling Huang, Yongchao Xie, Lingguang Yang, Wenhe Wang, Peiyi Wang, Yi Zhang, Maojun Yang, Yue Feng
Summary: The study reveals that AcrIF14 interacts with the Csy complex to prevent the hybridization of target DNA to crRNA and enables the Csy complex to interact with non-sequence-specific dsDNA. The PAM recognition loop of the Cas8f subunit and electropositive patches within the N-terminal domain of AcrIF14 are crucial for this interaction, different from the mechanism of AcrIF9.
NUCLEIC ACIDS RESEARCH
(2021)
Review
Biochemistry & Molecular Biology
Hongjun Yu, Gerrit J. Schut, Domink K. Haja, Michael W. W. Adams, Huilin Li
Summary: Modern respiratory complex I, MBH, and MBS likely share a common ancestor and help conserve energy in the Proterozoic era. They may have evolved from an integration of ancestral resistance and pH antiporters and redox-active modules. Recent high-resolution cryo-EM studies have greatly enhanced our understanding of their structures and evolutionary relationships.
JOURNAL OF BIOLOGICAL CHEMISTRY
(2021)
Article
Biochemistry & Molecular Biology
Xi Liu, Laixing Zhang, Yu Xiu, Teng Gao, Ling Huang, Yongchao Xie, Lingguang Yang, Wenhe Wang, Peiyi Wang, Yi Zhang, Maojun Yang, Yue Feng
Summary: The study reveals how AcrIF14 interacts with the Csy complex, blocking target DNA from binding to crRNA and enabling the Csy complex to interact with non-sequence-specific dsDNA. The PAM recognition loop of the Cas8f subunit and electropositive patches in the N-terminal domain of AcrIF14 are essential for this interaction, different from the mechanism of AcrIF9.
NUCLEIC ACIDS RESEARCH
(2021)
Article
Chemistry, Multidisciplinary
Yasuhiro Arikawa, Motoki Yamada, Nobuko Takemoto, Takuya Nagaoka, Yusuke Tsujita, Taiji Nakamura, Yusuke Tsuruta, Shinnosuke Horiuchi, Eri Sakuda, Kazunari Yoshizawa, Keisuke Umakoshi
Summary: Sulfite reduction is a crucial process in the global sulfur cycle, and it can be achieved using transition-metal complexes. In our study, we successfully simulated and achieved the stepwise reduction of sulfite from sulfite to sulfur monoxide, then to disulfide, and finally to hydrogen sulfide using a dinuclear ruthenium complex.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2023)
Article
Biochemistry & Molecular Biology
Marios Mejdani, April Pawluk, Karen L. Maxwell, Alan R. Davidson
Summary: Anti-CRISPRs are a diverse class of protein inhibitors produced by phages and mobile genetic elements to evade destruction by the CRISPR-Cas system. A study focused on AcrIE2, an anti-CRISPR inhibiting the Pseudomonas aeruginosa type I-E CRISPR-Cas system, revealed its unique ability to bind to the CRISPR-Cas complex without preventing DNA-binding, operating through a distinct mechanism compared to other type I anti-CRISPRs. AcrIE2 likely blocks DNA cleavage by inhibiting the recruitment of the Cas3 nuclease to the Cascade complex.
JOURNAL OF MOLECULAR BIOLOGY
(2021)
Article
Plant Sciences
Helene Roehricht, Jonathan Przybyla-Toscano, Joachim Forner, Clement Boussardon, Olivier Keech, Nicolas Rouhier, Etienne H. Meyer
Summary: This study identified an atypical mitochondrial ferredoxin (mFDX-like) that plays a crucial role in the assembly of complex I and formation of complex I-containing supercomplexes.
Article
Multidisciplinary Sciences
Yingke Liang, Alicia Plourde, Stephanie A. Bueler, Jun Liu, Peter Brzezinski, Siavash Vahidi, John L. Rubinstein
Summary: Oxidative phosphorylation is a promising target for treating Mycobacterium tuberculosis and other mycobacteria infections. The structure of the mycobacterial electron transport chain reveals the presence of several important components, including the orphan protein MSMEG_2064, acyl phosphati-dylinositol dimannoside, menaquinone, and a purine nucleoside triphosphate. These findings provide insights into the function and structure of the enzyme.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
(2023)
Article
Chemistry, Multidisciplinary
Hyunho Kim, Patricia Saura, Maximilian C. C. Poverlein, Ana P. Gamiz-Hernandez, Ville R. I. Kaila
Summary: Complex I is a redox-driven proton pump that powers oxidative phosphorylation. The mechanism of how redox reactions in Complex I trigger proton pumping remains unclear. In this study, we show that proton-coupled electron transfer reactions in Complex I induce long-range conformational changes and establish a proton pathway, which is responsible for proton pumping. Our findings provide insights into the catalytic control of protein conformational changes and ion transport across biological membranes.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2023)
Article
Multidisciplinary Sciences
Jing-Xiang Wu, Rui Liu, Kangcheng Song, Lei Chen
Summary: This study presents the cryo-EM structures of the human DUOX1-DUOXA1 complex in different calcium ion concentrations, revealing the symmetrical hetero-tetramer structure of DUOX1 stabilized by calcium ions. The presence of calcium ions enhances the catalytic activity of DUOX by stabilizing the dehydrogenase domain in a conformation that allows electron transfer.
NATURE COMMUNICATIONS
(2021)
Article
Biochemistry & Molecular Biology
Niklas Klusch, Jennifer Senkler, Oezkan Yildiz, Werner Kuehlbrandt, Hans-Peter Braun
Summary: Mitochondrial complex I is the main site for electron transfer and proton gradient generation. It is composed of two arms and a bridge domain, with different conformations and angles potentially regulating its activity.
Article
Biochemistry & Molecular Biology
Domen Kampjut, Leonid A. Sazanov
Summary: In this review, the importance, structure, and mechanisms of complex I in respiratory processes are discussed. By comparing structural evidence and mutagenesis data from different species, the mechanisms of electron transfer and proton pumping are elucidated, and the structural basis of deactivation phenomenon in complex I is explained.
CURRENT OPINION IN STRUCTURAL BIOLOGY
(2022)
Article
Multidisciplinary Sciences
Thomas D. Jackson, Jordan J. Crameri, Linden Muellner-Wong, Ann E. Frazier, Catherine S. Palmer, Luke E. Formosa, Daniella H. Hock, Kenji M. Fujihara, Tegan Stait, Alice J. Sharpe, David R. Thorburn, Michael T. Ryan, David A. Stroud, Diana Stojanovski
Summary: Sideroflexins (SFXNs) are a family of proteins that have different functions in mitochondrial biology. Loss of SFXN4 leads to complex I assembly defect and it interacts with the core components of the mitochondrial complex I intermediate assembly complex.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
(2022)
Article
Chemistry, Multidisciplinary
Oleksii Zdorevskyi, Amina Djurabekova, Jonathan Lasham, Vivek Sharma
Summary: Respiratory complex I is an redox-driven proton pump that contributes to mitochondrial ATP generation. The recent cryo-EM structural data revealed the positions of water molecules in the membrane domain of the complex, but the flow of protons in the membrane-bound subunits is still unclear. Computer simulations on high-resolution structural data show that protons can travel through the antiporter-like subunits, including at the subunit-subunit interface parallel to the membrane. Our simulations also demonstrate the role of conserved tyrosine residues and electrostatic effects in facilitating proton transfer. These results challenge prevailing proton pumping models of respiratory complex I.
Article
Biochemistry & Molecular Biology
Daniel N. Grba, James N. Blaza, Hannah R. Bridges, Ahmed-Noor A. Agip, Zhan Yin, Masatoshi Murai, Hideto Miyoshi, Judy Hirst
Summary: Mitochondrial complex I is a crucial enzyme in energy metabolism and plays a key role in ATP synthesis. This study reveals the structure of mouse complex I with a tight-binding acetogenin inhibitor, providing insights into the binding mode and structure-activity relationships. The amphipathic nature of the channel supports both tight binding of the inhibitor and rapid exchange of the substrate and product.
JOURNAL OF BIOLOGICAL CHEMISTRY
(2022)
Review
Biochemistry & Molecular Biology
Etienne Galemou Yoga, Heike Angerer, Kristian Parey, Volker Zickermann
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
(2020)
Article
Multidisciplinary Sciences
Igor Tascon, Joana S. Sousa, Robin A. Corey, Deryck J. Mills, David Griwatz, Nadine Aumueller, Vedrana Mikusevic, Phillip J. Stansfeld, Janet Vonck, Inga Haenelt
NATURE COMMUNICATIONS
(2020)
Article
Multidisciplinary Sciences
Rebecca Ebenhoch, Simone Prinz, Susann Kaltwasser, Deryck J. Mills, Robert Meinecke, Martin Ruebbelke, Dirk Reinert, Margit Bauer, Lisa Weixler, Markus Zeeb, Janet Vonck, Herbert Nar
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
(2020)
Article
Multidisciplinary Sciences
Etienne Galemou Yoga, Kristian Parey, Amina Djurabekova, Outi Haapanen, Karin Siegmund, Klaus Zwicker, Vivek Sharma, Volker Zickermann, Heike Angerer
NATURE COMMUNICATIONS
(2020)
Article
Microbiology
Tadeo Moreno Chicano, Lea Dietrich, Naomi M. de Almeida, Mohd Akram, Elisabeth Hartmann, Franziska Leidreiter, Daniel Leopoldus, Melanie Mueller, Ricardo Sanchez, Guylaine H. L. Nuijten, Joachim Reimann, Kerstin-Aniko Seifert, Ilme Schlichting, Laura van Niftrik, Mike S. M. Jetten, Andreas Dietl, Boran Kartal, Kristian Parey, Thomas R. M. Barends
Summary: The NXR multiprotein complex is a key enzyme in the nitrogen cycle, catalyzing both nitrite oxidation and nitrate reduction. This study provides structural and biochemical characterization of NXR from anammox bacteria, revealing the assembly and function of the complex. The results also uncover unexpected features in the enzyme's active site, cofactor coordination, and electron transfer pathways within the complex.
NATURE MICROBIOLOGY
(2021)
Article
Multidisciplinary Sciences
Kristian Parey, Jonathan Lasham, Deryck J. Mills, Amina Djurabekova, Outi Haapanen, Etienne Galemou Yoga, Hao Xie, Werner Kuhlbrandt, Vivek Sharma, Janet Vonck, Volker Zickermann
Summary: Mitochondrial NADH:ubiquinone oxidoreductase (complex I) is a 1-MDa membrane protein complex involved in energy metabolism. The complex drives proton translocation through redox reactions, contributing to the proton motive force for ATP synthase. Multiple structures of complex I have been determined, shedding light on its catalytic mechanism and proton pumping mechanism.
Article
Biochemistry & Molecular Biology
Iram Aziz, Susann Kaltwasser, Kanwal Kayastha, Radhika Khera, Janet Vonck, Ulrich Ermler
Summary: This study explored the structural diversity of W-based polyoxometalate clusters and found various POM cluster structures loaded with tungstate under different conditions. These structures contain different types and numbers of WOx units, displaying differences in stability and size.
JOURNAL OF INORGANIC BIOCHEMISTRY
(2022)
Article
Multidisciplinary Sciences
Laura Galazzo, Gianmarco Meier, Dovile Januliene, Kristian Parey, Dario De Vecchis, Bianca Striednig, Hubert Hilbi, Lars Schaefer, Ilya Kuprov, Arne Moeller, Enrica Bordignon, Markus A. Seeger
Summary: To truly understand the properties of membrane proteins in a physiological environment, it is necessary to study them within living cells. A study using a spin-labeled nanobody found that the wide inward-open conformation of the ABC transporter MsbA is prominently populated in Escherichia coli cells.
Article
Multidisciplinary Sciences
Jonathan Schiller, Eike Laube, Ilka Wittig, Werner Kuehlbrandt, Janet Vonck, Volker Zickermann
Summary: Cryo-electron microscopy was used to determine the structure of assembly intermediates associated with NDUFAF1. It was found that NDUFAF1, together with ND2, NDUFC2, and CIA84, forms the nucleation point of the assembly pathway. The central subunit ND3 is locked in an assembly-competent conformation by NDUFAF1, and major rearrangements of central subunits are required for complex I maturation.
Article
Multidisciplinary Sciences
Michael F. Fuss, Jan-Philip Wieferig, Robin A. Corey, Yvonne Hellmich, Igor Tascon, Joana S. Sousa, Phillip J. Stansfeld, Janet Vonck, Inga Haenelt
Summary: Cyclic di-AMP inhibits the potassium transporter KimA by reducing the mobility of transmembrane helices at the cytosolic side of the K+ binding site, trapping KimA in an inward-occluded conformation. This study provides insights into how the second messenger cyclic di-AMP regulates bacterial physiology.
NATURE COMMUNICATIONS
(2023)
Article
Multidisciplinary Sciences
Laura F. Fielden, Jakob D. Busch, Sandra G. Merkt, Iniyan Ganesan, Conny Steiert, Hanna B. Hasselblatt, Jon V. Busto, Christophe Wirth, Nicole Zufall, Sibylle Jungbluth, Katja Noll, Julia M. Dung, Ludmila Butenko, Karina von der Malsburg, Hans-Georg Koch, Carola Hunte, Martin van der Laan, Nils Wiedemann
Summary: The presequence translocase of the mitochondrial inner membrane (TIM23) is the major route for importing nuclear-encoded proteins into mitochondria. Tim17, a subunit of TIM23, interacts with preproteins in the matrix or inner membrane for protein translocation. The negative charges in Tim17 initiate the translocation mechanism and release the preproteins into the inner membrane.
Article
Biochemistry & Molecular Biology
Jann-Louis Hau, Susann Kaltwasser, Valentin Muras, Marco S. Casutt, Georg Vohl, Bjoern Claussen, Wojtek Steffen, Alexander Leitner, Eckhard Bill, George E. Cutsail, Serena Debeer, Janet Vonck, Julia Steuber, Guenter Fritz
Summary: This study reveals that ion pumping in Na+-NQR is driven by large conformational changes coupling electron transfer to ion translocation. This mechanism is of significant importance for NADH oxidation in the human pathogen Vibrio cholerae.
NATURE STRUCTURAL & MOLECULAR BIOLOGY
(2023)
Article
Multidisciplinary Sciences
Jan-Hannes Schaefer, Carolin Koerner, Bianca M. Esch, Sergej Limar, Kristian Parey, Stefan Walter, Dovile Januliene, Arne Moeller, Florian Froehlich
Summary: This study presents the high-resolution cryo-EM structures of the yeast SPT complex with Tsc3, Orm1, and Sac1. The interaction between ceramide and Orm1 is found to inhibit the activity of yeast SPT. Furthermore, the binding of ceramide and ergosterol suggests a co-regulation of sphingolipid biogenesis and sterol metabolism within the SPOTS complex.
NATURE COMMUNICATIONS
(2023)
