Assuming you meant cation and not action, gallium would most likely form a cation because it is a group A element
Answer:
Explanation:
Your strategy here will be to
use the chemical formula of carbon dioxide to find the number of molecules of
CO
2
that would contain that many atoms of oxygen
use Avogadro's constant to convert the number of molecules to moles of carbon dioxide
use the molar mass of carbon dioxide to convert the moles to grams
So, you know that one molecule of carbon dioxide contains
one atom of carbon,
1
×
C
two atoms of oxygen,
2
×
O
This means that the given number of atoms of oxygen would correspond to
4.8
⋅
10
22
atoms O
⋅
1 molecule CO
2
2
atoms O
=
2.4
⋅
10
22
molecules CO
2
Now, one mole of any molecular substance contains exactly
6.022
⋅
10
22
molecules of that substance -- this is known as Avogadro's constant.
In your case, the sample of carbon dioxide molecules contains
2.4
⋅
10
22
molecules CO
2
⋅
1 mole CO
2
6.022
⋅
10
23
molecules CO
2
=
0.03985 moles CO
2
Finally, carbon dioxide has a molar mass of
44.01 g mol
−
1
, which means that your sample will have a mass of
0.03985
moles CO
2
⋅
44.01 g
1
mole CO
2
=
¯¯¯¯¯¯¯¯¯¯¯¯¯¯¯¯¯
∣
∣
a
a
1.8 g
a
a
∣
∣
−−−−−−−−−
The answer is rounded to two sig figs, the number of sig figs you have for the number of atoms of oxygen present in the sample.
Answer: Mass
<em>Input:</em> Mass is a measure of the quantity of matter in an object.
Explanation: Mass is the measure of amount of matter in a certain object.
Wait, do you mind clarifying what you would like answered for the question?
The production of manganese peroxidase (MnP) by Irpex lacteus, purified to electrophoretic homogeneity by acetone precipitation, HiPrep Q and HiPrep Sephacryl S-200 chromatography, was shown to correlate with the decolorization of textile industry wastewater. The MnP was purified 11.0-fold, with an overall yield of 24.3%. The molecular mass of the native enzyme, as determined by gel filtration chromatography, was about 53 kDa. The enzyme was shown to have a molecular mass of 53.2 and 38.3 kDa on SDS-PAGE and MALDI-TOF mass spectrometry, respectively, and an isoelectric point of about 3.7. The enzyme was optimally active at pH 6.0 and between 30 and 40 degrees C. The enzyme efficiently catalyzed the decolorization of various artificial dyes and oxidized Mn (II) to Mn (III) in the presence of H(2)O(2). The absorption spectrum of the enzyme exhibited maxima at 407, 500, and 640 nm. The amino acid sequence of the three tryptic peptides was analyzed by ESI Q-TOF MS/MS spectrometry, and showed low similarity to those of the extracellular peroxidases of other white-rot basidiomycetes.
