Page last updated: 2024-08-21

n-hexadecane and heme

n-hexadecane has been researched along with heme in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Bombelli, P; Cheng, Q; Liu, HT; Sanglard, D; Slabas, AR; Smith, A; Vanhanen, S	1
Goswami, P; Kumar, AK; Vatsyayan, P	1

Other Studies

2 other study(ies) available for n-hexadecane and heme

Article	Year
Candida yeast long chain fatty alcohol oxidase is a c-type haemoprotein and plays an important role in long chain fatty acid metabolism. Biochimica et biophysica acta, 2005, Aug-15, Volume: 1735, Issue:3 Topics: Alcohol Oxidoreductases; Alkanes; Amino Acid Sequence; Binding Sites; Candida tropicalis; Conserved Sequence; Fatty Acids, Nonesterified; Fungal Proteins; Heme; Hemeproteins; Kinetics; Mitochondria; Models, Biological; Molecular Sequence Data; Palmitic Acid; Plasmids; Polymerase Chain Reaction; Sequence Alignment; Sequence Homology, Amino Acid; Substrate Specificity	2005
Broad substrate Cytochrome P450 monooxygenase activity in the cells of Aspergillus terreus MTCC 6324. Bioresource technology, 2008, Volume: 99, Issue:1 Topics: Acetone; Alkanes; Aspergillus; Cytochrome P-450 Enzyme System; Dimethyl Sulfoxide; Electrophoresis, Polyacrylamide Gel; Heme; Hydrogen-Ion Concentration; Methanol; Microsomes; Mitochondria; Mixed Function Oxygenases; Molecular Weight; Naphthalenes; Oxidation-Reduction; Spectrophotometry; Substrate Specificity; Temperature; Time Factors	2008

Article

Year

Candida yeast long chain fatty alcohol oxidase is a c-type haemoprotein and plays an important role in long chain fatty acid metabolism.

Biochimica et biophysica acta, 2005, Aug-15, Volume: 1735, Issue:3

Topics: Alcohol Oxidoreductases; Alkanes; Amino Acid Sequence; Binding Sites; Candida tropicalis; Conserved Sequence; Fatty Acids, Nonesterified; Fungal Proteins; Heme; Hemeproteins; Kinetics; Mitochondria; Models, Biological; Molecular Sequence Data; Palmitic Acid; Plasmids; Polymerase Chain Reaction; Sequence Alignment; Sequence Homology, Amino Acid; Substrate Specificity

2005

Broad substrate Cytochrome P450 monooxygenase activity in the cells of Aspergillus terreus MTCC 6324.

Bioresource technology, 2008, Volume: 99, Issue:1

Topics: Acetone; Alkanes; Aspergillus; Cytochrome P-450 Enzyme System; Dimethyl Sulfoxide; Electrophoresis, Polyacrylamide Gel; Heme; Hydrogen-Ion Concentration; Methanol; Microsomes; Mitochondria; Mixed Function Oxygenases; Molecular Weight; Naphthalenes; Oxidation-Reduction; Spectrophotometry; Substrate Specificity; Temperature; Time Factors

2008