GO_REF:0000024

Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity

GO_REF:0000033

Annotation inferences using phylogenetic trees

GO_REF:0000107

Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara

GO_REF:0000119

Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs

GO_REF:0000120

Combined Automated Annotation using Multiple IEA Methods

PMID:19468303

Lineage-specific biology revealed by a finished genome assembly of the mouse.

Provides the genomic sequence for Ndufb1 from mouse strain C57BL/6J

"we are now able to define 20,210 protein-coding genes"

PMID:30030361

Assembly of mammalian oxidative phosphorylation complexes I-V and supercomplexes.

Review covering assembly pathways of OXPHOS complexes including Complex I

"The assembly of the five oxidative phosphorylation system (OXPHOS) complexes in the inner mitochondrial membrane is an intricate process"
Complex I assembly involves modular intermediates with accessory subunits playing essential roles in assembly, regulation and stability

"The human enzymes comprise core proteins, performing the catalytic activities, and a large number of 'supernumerary' subunits that play essential roles in assembly, regulation and stability"

PMID:38575788

SCAF1 drives the compositional diversity of mammalian respirasomes.

Cryo-EM structures of three types of mouse respirasomes resolved at 3.3-3.6 A, with Ndufb1 visible as chain f in Complex I

"mammalian (mouse) tissues contain three defined types of 'respirasome', supercomplexes made of CI, CIII2 and CIV"
SCAF1 is associated with one type of respirasome, demonstrating compositional diversity of supercomplexes

"The stoichiometry and position of CIV differs in the three respirasomes, of which only one contains the supercomplex-associated factor SCAF1"

PMID:27626371

Accessory subunits are integral for assembly and function of human mitochondrial complex I.

Systematic CRISPR knockout of all 31 accessory subunits shows they are essential for Complex I assembly and function

"Complex I (NADH:ubiquinone oxidoreductase) is the first enzyme of the mitochondrial respiratory chain and is composed of 45 subunits in humans"

file:mouse/Ndufb1/Ndufb1-notes.md

Research notes on Ndufb1

NDUFB1 is part of the ND4-module assembly intermediate in the modular Complex I assembly pathway
BioReason deep research contains errors including confusion of Complex I with Complex III assembly and NDUFB1 with NDUFAB1

file:mouse/Ndufb1/Ndufb1-deep-research-falcon.md

Falcon (Edison) deep research report on mouse Ndufb1 (P0DN34)

NDUFB1 is a non-catalytic accessory structural subunit of mitochondrial Complex I, not a redox-cofactor-bearing catalytic subunit.

"**NDUFB1 (Ndufb1 in mouse)** is an **accessory (non-catalytic) structural subunit** rather than a redox cofactor–bearing catalytic subunit."
NDUFB1 is placed in the membrane-arm distal P-module, specifically the ND4 module, so it functions at the inner mitochondrial membrane.

"NDUFB1 is consistently placed in the **membrane-arm distal P-module**, specifically the **ND4 module**"
The ND4 module comprises mtDNA-encoded ND4 plus accessory subunits NDUFB1, NDUFB5, NDUFB10, and NDUFB11.

"**ND4 module** includes **ND4 (mtDNA-encoded)** plus accessory subunits including **NDUFB1, NDUFB5, NDUFB10, NDUFB11**."
Complexome profiling detected the NDUFB1-containing ND4 module as a ~260 kDa assembly intermediate, supporting modular assembly.

"the **ND4 module** (explicitly including **NDUFB1**) was **detected as an assembly intermediate** with an apparent size of approximately **~260 kDa**"
Order-of-assembly evidence places NDUFB1 as a later addition to the ND4 module, after an NDUFB5/NDUFB6/NDUFB10/NDUFB11 subcomplex assembles.

"a subcomplex containing **NDUFB5, NDUFB6, NDUFB10, NDUFB11** is described as assembling early, followed by the addition of **NDUFB1** and **ND4**"
Knockout/assembly review evidence indicates NDUFB1 is needed for stabilization of membrane-arm subassemblies, with its loss blocking Complex I assembly and reducing assembled-enzyme abundance.

"NDUFB1 loss blocks complex I assembly and reduces abundance of assembled enzyme"
The PD-a/ND4 membrane-arm module containing NDUFB1 is specifically required for respirasome (supercomplex) assembly.

"Perturbation of the PD-a module (the module containing NDUFB1) impaired respirasome assembly"
Complex I transfers electrons from NADH to ubiquinone and couples this to proton translocation across the inner mitochondrial membrane; NDUFB1 contributes structurally to formation of this mature enzyme.

"It transfers electrons from **NADH to ubiquinone (CoQ)** and couples this redox reaction to **proton translocation across the inner mitochondrial membrane (IMM)**"