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Phase separation of FSP1 promotes ferroptosis
An inhibitor of the ferroptosis-suppressing FSP1 induces phase separation of FSP1, thereby impairing its function and reducing tumour growth.
- Toshitaka Nakamura
- , Clara Hipp
- & Marcus Conrad
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Article |
Multifunctional biocatalyst for conjugate reduction and reductive amination
A biocatalytic enzyme originating from bacteria, EneIRED, facilitates amine-activated conjugate alkene reduction followed by reductive amination, efficiently preparing chiral amine diastereomers, which are commonly used in pharmaceuticals and agrochemicals.
- Thomas W. Thorpe
- , James R. Marshall
- & Nicholas J. Turner
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Article |
The polar oxy-metabolome reveals the 4-hydroxymandelate CoQ10 synthesis pathway
18O2 labelling is used to identify metabolites in human cells that incorporate gaseous oxygen, including 4-hydroxymandelate, an intermediate in the synthesis of the coenzyme Q10 head group.
- Robert S. Banh
- , Esther S. Kim
- & Michael E. Pacold
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Letter |
Singlet molecular oxygen regulates vascular tone and blood pressure in inflammation
Singlet molecular oxygen, produced by indoleamine 2,3-dioxygenase 1 activity, gives rise to a signalling molecule that regulates arterial relaxation under inflammatory conditions.
- Christopher P. Stanley
- , Ghassan J. Maghzal
- & Roland Stocker
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Letter |
Metal-free ribonucleotide reduction powered by a DOPA radical in Mycoplasma pathogens
A subclass of ribonucleotide reductase in Mycoplasma pathogens contains a stable radical formed from a modified tyrosine residue, overturning the presumed requirement for a dinuclear metal site in aerobic ribonucleotide reductase.
- Vivek Srinivas
- , Hugo Lebrette
- & Martin Högbom
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Letter |
Structure of mammalian respiratory complex I
Electron cryomicroscopy structures are provided for all core and supernumerary protein subunits of mammalian complex I, a 45-subunit enzyme that powers eukaryotic respiration.
- Jiapeng Zhu
- , Kutti R. Vinothkumar
- & Judy Hirst
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Letter |
Repairing oxidized proteins in the bacterial envelope using respiratory chain electrons
The identification of an enzymatic system repairing proteins containing oxidized methionine in the bacterial cell envelope, a compartment particularly susceptible to oxidative damage by host defence mechanisms.
- Alexandra Gennaris
- , Benjamin Ezraty
- & Frédéric Barras
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Letter |
X-ray structure of a mammalian stearoyl-CoA desaturase
The crystal structure of mouse SCD1 bound to fatty acid stearoyl-CoA is solved at 2.6 Å resolution; the structure reveals a novel geometry for the dimetal centre, and the acyl chain of the bound fatty acid is shown to be shielded and shaped to a particular conformation by the enzyme, providing a structural basis for the selectivity of fatty acid metabolism.
- Yonghong Bai
- , Jason G. McCoy
- & Ming Zhou
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Letter |
Trace-gas metabolic versatility of the facultative methanotroph Methylocella silvestris
Distinct groups of microorganisms have been thought to grow on methane and on short-chain alkanes; now, the methanotroph Methylocella silvestris is shown to express two distinct soluble di-iron centre monooxygenases that allow it to use either methane or propane as a carbon and energy source.
- Andrew T. Crombie
- & J. Colin Murrell
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Research Highlights |
Enzyme design inspired by cancer
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Letter |
Structure of a methyl-coenzyme M reductase from Black Sea mats that oxidize methane anaerobically
The crystal structure of the enzyme MCR from methanogenic archaea shows that it is very similar to that of methanotrophic archaea; the differences observed may tune the enzymes for their respective biological context within the sea mats.
- Seigo Shima
- , Martin Krueger
- & Ulrich Ermler
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Letter |
Reductive glutamine metabolism by IDH1 mediates lipogenesis under hypoxia
- Christian M. Metallo
- , Paulo A. Gameiro
- & Gregory Stephanopoulos
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Letter |
The crystal structure of an oxygen-tolerant hydrogenase uncovers a novel iron-sulphur centre
- Johannes Fritsch
- , Patrick Scheerer
- & Christian M. T. Spahn
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Letter |
N2O binding at a [4Cu:2S] copper–sulphur cluster in nitrous oxide reductase
- Anja Pomowski
- , Walter G. Zumft
- & Oliver Einsle
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Letter |
X-ray crystal structure of the light-independent protochlorophyllide reductase
The ability of plants to 'green' in the dark is attributed to the activity of the dark-operative protochlorophyllide oxidoreductase (DPOR). This enzyme catalyses the stereospecific reduction of the C17≡C18 double bond of protochlorophyllide to form chlorophyllide a, the direct precursor of chlorophyll a. The X-ray crystal structure of the catalytic component of DPOR has now been solved. A chemical mechanism is proposed by which the reduction of the double bond may occur.
- Norifumi Muraki
- , Jiro Nomata
- & Yuichi Fujita
DHODH inhibitors sensitize to ferroptosis by FSP1 inhibition